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Conserved domains on  [gi|564400362|ref|XP_006257462|]
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rac GTPase-activating protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
345-538 2.21e-119

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: 352.37  E-value: 2.21e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 345 IGEGMLADFVSQTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDdIHAICSLLKDF 424
Cdd:cd04382    1 IGTGELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVD-IHVICGCLKDF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 425 LRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQSPSTKMDVVNLAKIFGPTIV 504
Cdd:cd04382   80 LRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTIV 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 564400362 505 AHTVPNPDPVTMFQDIKRQLKVVERLLSLPLEYW 538
Cdd:cd04382  160 GYSVPNPDPMTILQDTVRQPRVVERLLEIPSDYW 193
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
284-337 2.24e-27

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: 104.80  E-value: 2.24e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564400362 284 RLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRLVSHPECRDRCPLPCIPP 337
Cdd:cd20821    1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPT 54
Tropomyosin super family cl37621
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
43-108 2.87e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


The actual alignment was detected with superfamily member pfam00261:

Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 39.63  E-value: 2.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362   43 KKCQRTNQELEKFKDLLLKAETgrsaldvKLKHARnqvdveiKRRQRAEAECAKLEQQIQLIRDIL 108
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMK-------KLEEAE-------KRAEKAEAEVAALNRRIQLLEEEL 52
 
Name Accession Description Interval E-value
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
345-538 2.21e-119

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: 352.37  E-value: 2.21e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 345 IGEGMLADFVSQTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDdIHAICSLLKDF 424
Cdd:cd04382    1 IGTGELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVD-IHVICGCLKDF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 425 LRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQSPSTKMDVVNLAKIFGPTIV 504
Cdd:cd04382   80 LRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTIV 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 564400362 505 AHTVPNPDPVTMFQDIKRQLKVVERLLSLPLEYW 538
Cdd:cd04382  160 GYSVPNPDPMTILQDTVRQPRVVERLLEIPSDYW 193
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
362-506 1.26e-53

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 180.05  E-value: 1.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362  362 PAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFWLSKAF 441
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362  442 MEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVAH 506
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQnSDVNKMNAHNLAIVFGPTLLRP 146
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
359-532 9.35e-49

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: 167.83  E-value: 9.35e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362   359 PMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLK-VKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFWL 437
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYD-VHDVAGLLKLFLRELPEPLITYEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362   438 SKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIvahTVPNPDPVTM 516
Cdd:smart00324  80 YEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTL---LRPPDGEVAS 156
                          170
                   ....*....|....*.
gi 564400362   517 FQDIKRQLKVVERLLS 532
Cdd:smart00324 157 LKDIRHQNTVIEFLIE 172
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
284-337 2.24e-27

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: 104.80  E-value: 2.24e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564400362 284 RLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRLVSHPECRDRCPLPCIPP 337
Cdd:cd20821    1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPT 54
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
286-334 7.32e-07

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: 46.31  E-value: 7.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564400362   286 HDFVSKTVIKPESCVPCGKRIKFG-KLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSfKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
286-336 2.76e-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: 44.74  E-value: 2.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564400362  286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPCIP 336
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWgLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
43-108 2.87e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 39.63  E-value: 2.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362   43 KKCQRTNQELEKFKDLLLKAETgrsaldvKLKHARnqvdveiKRRQRAEAECAKLEQQIQLIRDIL 108
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMK-------KLEEAE-------KRAEKAEAEVAALNRRIQLLEEEL 52
 
Name Accession Description Interval E-value
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
345-538 2.21e-119

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: 352.37  E-value: 2.21e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 345 IGEGMLADFVSQTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDdIHAICSLLKDF 424
Cdd:cd04382    1 IGTGELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVD-IHVICGCLKDF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 425 LRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQSPSTKMDVVNLAKIFGPTIV 504
Cdd:cd04382   80 LRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTIV 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 564400362 505 AHTVPNPDPVTMFQDIKRQLKVVERLLSLPLEYW 538
Cdd:cd04382  160 GYSVPNPDPMTILQDTVRQPRVVERLLEIPSDYW 193
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
362-506 1.26e-53

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 180.05  E-value: 1.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362  362 PAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFWLSKAF 441
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362  442 MEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVAH 506
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQnSDVNKMNAHNLAIVFGPTLLRP 146
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
359-532 9.35e-49

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: 167.83  E-value: 9.35e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362   359 PMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLK-VKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFWL 437
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYD-VHDVAGLLKLFLRELPEPLITYEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362   438 SKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIvahTVPNPDPVTM 516
Cdd:smart00324  80 YEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTL---LRPPDGEVAS 156
                          170
                   ....*....|....*.
gi 564400362   517 FQDIKRQLKVVERLLS 532
Cdd:smart00324 157 LKDIRHQNTVIEFLIE 172
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
362-532 2.01e-45

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: 158.62  E-value: 2.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 362 PAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFWLSKAF 441
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYD-VHDVASLLKLYLRELPEPLIPFELYDEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 442 MEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVahtVPNPDPVTMFQDI 520
Cdd:cd00159   80 IELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQnSEVNKMTASNLAIVFAPTLL---RPPDSDDELLEDI 156
                        170
                 ....*....|..
gi 564400362 521 KRQLKVVERLLS 532
Cdd:cd00159  157 KKLNEIVEFLIE 168
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
360-531 9.51e-41

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: 146.78  E-value: 9.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 360 MIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLK-VKTVPLLSKVD---DIHAICSLLKDFLRNLKEPLLTF 435
Cdd:cd04398   15 NVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKdPLNVLLISPEDyesDIHSVASLLKLFFRELPEPLLTK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 436 WLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQSPS-TKMDVVNLAKIFGPTIVahtvpnPDPV 514
Cdd:cd04398   95 ALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESvNRMSVNNLAIIWGPTLM------NAAP 168
                        170
                 ....*....|....*..
gi 564400362 515 TMFQDIKRQLKVVERLL 531
Cdd:cd04398  169 DNAADMSFQSRVIETLL 185
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
355-531 5.33e-35

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


Pssm-ID: 239860  Cd Length: 196  Bit Score: 130.98  E-value: 5.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 355 SQTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLK-VKTVPLLS-KVDDIHAICSLLKDFLRNLKEPL 432
Cdd:cd04395   12 SSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRgGFDIDLQDpRWRDVNVVSSLLKSFFRKLPEPL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 433 LTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVahTVPNP 511
Cdd:cd04395   92 FTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADnSEVNKMEPRNLAIVFGPTLV--RTSDD 169
                        170       180
                 ....*....|....*....|
gi 564400362 512 DPVTMFQDIKRQLKVVERLL 531
Cdd:cd04395  170 NMETMVTHMPDQCKIVETLI 189
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
361-532 1.34e-32

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: 124.17  E-value: 1.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLK--VKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFWLS 438
Cdd:cd04372   16 RPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdgEKADISATVYPDINVITGALKLYFRDLPIPVITYDTY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 439 KAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVAhtVPNPDPVTMF 517
Cdd:cd04372   96 PKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLhEKDNKMNAENLGIVFGPTLMR--PPEDSALTTL 173
                        170
                 ....*....|....*
gi 564400362 518 QDIKRQLKVVERLLS 532
Cdd:cd04372  174 NDMRYQILIVQLLIT 188
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
350-531 7.56e-31

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


Pssm-ID: 239842  Cd Length: 186  Bit Score: 119.08  E-value: 7.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 350 LADFVSQTSPmIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKflkVKTVPLLSKVDD--IHAICSLLKDFLRN 427
Cdd:cd04377    5 LSSLTSEDRS-VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQG---LDTDPDSVNLEDypIHVITSVLKQWLRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 428 LKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVaH 506
Cdd:cd04377   81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVAlQEEVNRMSANALAIVFAPCIL-R 159
                        170       180
                 ....*....|....*....|....*
gi 564400362 507 TVPNPDPVTMFQDIKRQLKVVERLL 531
Cdd:cd04377  160 CPDTADPLQSLQDVSKTTTCVETLI 184
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
363-532 4.74e-29

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


Pssm-ID: 239839  Cd Length: 203  Bit Score: 114.41  E-value: 4.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 363 AIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKT-----VPLLSKVDDIHAICSLLKDFLRNLKEPLLTFWL 437
Cdd:cd04374   30 KFVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGLDPKTstpgdVDLDNSEWEIKTITSALKTYLRNLPEPLMTYEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 438 SKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVAhtvPNPDPVTM 516
Cdd:cd04374  110 HNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSdHSKKNLMTVSNLGVVFGPTLLR---PQEETVAA 186
                        170
                 ....*....|....*.
gi 564400362 517 FQDIKRQLKVVERLLS 532
Cdd:cd04374  187 IMDIKFQNIVVEILIE 202
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
361-503 9.22e-29

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: 113.17  E-value: 9.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLK-VKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFWLSK 439
Cdd:cd04385   15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKdARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHA 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564400362 440 AFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTI 503
Cdd:cd04385   95 EWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQkHSDENQMSVHNLALVFGPTL 159
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
361-532 1.44e-28

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: 113.29  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDiHAICSLLKDFLRNLKEPLLTFWLSKA 440
Cdd:cd04378   16 VPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSP-HDISSVLKLFLRQLPEPLILFRLYND 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 441 FMEAAEITDEDNSTAA--------------MYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVa 505
Cdd:cd04378   95 FIALAKEIQRDTEEDKapntpievnriirkLKDLLRQLPASNYNTLQHLIAHLYRVAeQFEENKMSPNNLGIVFGPTLI- 173
                        170       180
                 ....*....|....*....|....*....
gi 564400362 506 HTVPNPDPVTM--FQDIKRQLKVVERLLS 532
Cdd:cd04378  174 RPRPGDADVSLssLVDYGYQARLVEFLIT 202
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
356-533 1.51e-28

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: 112.71  E-value: 1.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 356 QTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKF-LKVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLT 434
Cdd:cd04387   11 RERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFdTNNKDVSVMLSEMDVNAIAGTLKLYFRELPEPLFT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 435 FWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVAHTVPNPDP 513
Cdd:cd04387   91 DELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAErEEVNKMSLHNLATVFGPTLLRPSEKESKI 170
                        170       180
                 ....*....|....*....|
gi 564400362 514 VTMFQDIKRQLKVVERLLSL 533
Cdd:cd04387  171 PTNTMTDSWSLEVMSQVQVL 190
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
284-337 2.24e-27

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: 104.80  E-value: 2.24e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564400362 284 RLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRLVSHPECRDRCPLPCIPP 337
Cdd:cd20821    1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPT 54
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
361-532 1.41e-26

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: 107.09  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPL-LSKVDDIHAICSLLKDFLRNLKEPLLTFWLSK 439
Cdd:cd04403   16 VPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLdDSKWEDIHVITGALKLFFRELPEPLFPYSLFN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 440 AFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVAHTVPNPDPV--TM 516
Cdd:cd04403   96 DFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEhGEKNRMTTQNLAIVFGPTLLRPEQETGNIAvhMV 175
                        170
                 ....*....|....*.
gi 564400362 517 FQDikrqlKVVERLLS 532
Cdd:cd04403  176 YQN-----QIVELILL 186
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
350-531 1.51e-26

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


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 107.00  E-value: 1.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 350 LADFVSQTSPmIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKflkVKTVPLLSKVDD--IHAICSLLKDFLRN 427
Cdd:cd04407    5 VGSLTSNKTS-VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQL---LQADPENVKLENypIHAITGLLKQWLRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 428 LKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVaH 506
Cdd:cd04407   81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVAlEEDVNRMSPNALAIVFAPCLL-R 159
                        170       180
                 ....*....|....*....|....*
gi 564400362 507 TVPNPDPVTMFQDIKRQLKVVERLL 531
Cdd:cd04407  160 CPDSSDPLTSMKDVAKTTTCVEMLI 184
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
337-503 4.29e-25

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: 103.31  E-value: 4.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 337 PLVGTPvkigegmLADFVSQTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKfLKVKTV--PLLSKVDDI 414
Cdd:cd04386    3 PVFGTP-------LEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAA-LDAGTFslPLDEFYSDP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 415 HAICSLLKDFLRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVV 493
Cdd:cd04386   75 HAVASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQkSDENKMSPS 154
                        170
                 ....*....|
gi 564400362 494 NLAKIFGPTI 503
Cdd:cd04386  155 NIAIVLAPNL 164
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
361-532 3.64e-24

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: 100.28  E-value: 3.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDiHAICSLLKDFLRNLKEPLLTFWLSKA 440
Cdd:cd04408   16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSP-HDITSVLKHFLKELPEPVLPFQLYDD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 441 FMEAAEITDEDNSTAA------------MYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVaHT 507
Cdd:cd04408   95 FIALAKELQRDSEKAAespsiveniirsLKELLGRLPVSNYNTLRHLMAHLYRVAeRFEDNKMSPNNLGIVFGPTLL-RP 173
                        170       180
                 ....*....|....*....|....*.
gi 564400362 508 VPNPD-PVTMFQDIKRQLKVVERLLS 532
Cdd:cd04408  174 LVGGDvSMICLLDTGYQAQLVEFLIS 199
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
356-512 1.64e-23

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


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 98.30  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 356 QTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLlSKVDDIHAICSLLKDFLRNLKEPLLTF 435
Cdd:cd04393   15 QPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDL-SKEADVCSAASLLRLFLQELPEGLIPA 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564400362 436 WLSKAFMEA-AEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVaHTVPNPD 512
Cdd:cd04393   94 SLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVAsQHHENRMTAENLAAVFGPDVF-HVYTDVE 171
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
350-516 2.09e-23

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: 97.91  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 350 LADFVSQTSPmIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDIHAICSLLKDFLRNLK 429
Cdd:cd04373    5 LANVVTSEKP-IPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFSELP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 430 EPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVahtv 508
Cdd:cd04373   84 DPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQnSKVNLMTSENLSICFWPTLM---- 159

                 ....*...
gi 564400362 509 pNPDPVTM 516
Cdd:cd04373  160 -RPDFTSM 166
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
359-503 2.21e-23

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: 98.28  E-value: 2.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 359 PMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVdDIHAICSLLKDFLRNLKEPLLTFWLS 438
Cdd:cd04376    7 RQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENH-SVHDVAALLKEFFRDMPDPLLPRELY 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564400362 439 KAFMEAAEITDEDNsTAAMYQAVSELPQANRDTLAFLMIHLQRVAQS------------PSTKMDVVNLAKIFGPTI 503
Cdd:cd04376   86 TAFIGTALLEPDEQ-LEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHaadsidedgqevSGNKMTSLNLATIFGPNL 161
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
361-503 3.55e-23

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: 97.43  E-value: 3.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIE-QRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLL--SKVDDIHAICSLLKDFLRNLKEPLLTFWL 437
Cdd:cd04400   22 LPSVVYRCIEYLDkNRAIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFssSLYPDVHTVAGLLKLYLRELPTLILGGEL 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564400362 438 SKAFMEAAEI-TDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRV-AQSPSTKMDVVNLAKIFGPTI 503
Cdd:cd04400  102 HNDFKRLVEEnHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIiEHSDVNKMNLRNVCIVFSPTL 169
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
360-516 7.25e-23

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


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 96.74  E-value: 7.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 360 MIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFlKVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFWLSK 439
Cdd:cd04390   21 LVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAF-DAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 440 AFMEAAEIT--DEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVAHTVpnPDPVTM 516
Cdd:cd04390  100 DFLSCAQLLskDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSnSSVNKMSVQNLATVFGPNILRPKV--EDPATI 177
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
350-503 1.17e-22

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: 96.03  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 350 LADFVSQTSPMIPAIVVSCVNEIEQRGLTEaGLYRISGCDRTVKELKEKFlKVKTVPLLSK---VDDIHAICSLLKDFLR 426
Cdd:cd04384    7 LTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEF-DSEQIPDLTKdvyIQDIHSVSSLCKLYFR 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564400362 427 NLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQSPS-TKMDVVNLAKIFGPTI 503
Cdd:cd04384   85 ELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSiTNMHAKNLAIVWAPNL 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
357-506 1.27e-22

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: 96.38  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 357 TSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSK--VDDIHAICSLLKDFLRNLKEPLLT 434
Cdd:cd04379   14 ESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEelYPDINVITGVLKDYLRELPEPLIT 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362 435 FWLSKAFMEAAEI---TDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVAH 506
Cdd:cd04379   94 PQLYEMVLEALAValpNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLsNSERNKMTPQNLAVCFGPVLMFC 169
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
361-503 4.75e-22

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


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 93.65  E-value: 4.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKvKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFWLSKA 440
Cdd:cd04381   20 LPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNR-RESPNLEEYE-PPTVASLLKQYLRELPEPLLTKELMPR 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564400362 441 FMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHL-QRVAQSPSTKMDVVNLAKIFGPTI 503
Cdd:cd04381   98 FEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMdHVIAQELETKMNIQNISIVLSPTV 161
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
351-531 3.97e-21

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: 92.18  E-value: 3.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 351 ADF--VSQTSP-MIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDiHAICSLLKDFLRN 427
Cdd:cd04409    3 ADFaqVAKKSPdGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSP-HDISNVLKLYLRQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 428 LKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVS----------------------ELPQANRDTLAFLMIHLQRVA-Q 484
Cdd:cd04409   82 LPEPLILFRLYNEFIGLAKESQHVNETQEAKKNSDkkwpnmctelnrillkskdllrQLPAPNYNTLQFLIVHLHRVSeQ 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564400362 485 SPSTKMDVVNLAKIFGPTIVaHTVPNPDPVTM--FQDIKRQLKVVERLL 531
Cdd:cd04409  162 AEENKMSASNLGIIFGPTLI-RPRPTDATVSLssLVDYPHQARLVELLI 209
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
360-504 6.91e-21

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: 90.86  E-value: 6.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 360 MIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLlSKVDDIHAICSLLKDFLRNLKEPLLTFWLSK 439
Cdd:cd04404   22 PIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDF-DQYEDVHLPAVILKTFLRELPEPLLTFDLYD 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362 440 AFMEAAEItDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIV 504
Cdd:cd04404  101 DIVGFLNV-DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAhSDQNKMTNSNLAVVFGPNLL 165
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
360-532 4.79e-20

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: 88.51  E-value: 4.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 360 MIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLlsKVDDIHAICSLLKDFLRNLKEPLLTFWLSK 439
Cdd:cd04402   14 NLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDL--KAEPVLLLASVLKDFLRNIPGSLLSSDLYE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 440 AFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQSPST-KMDVVNLAKIFGPTIVAhtvpNPDPVTMF- 517
Cdd:cd04402   92 EWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETnKMDAFNLAVCIAPSLLW----PPASSELQn 167
                        170
                 ....*....|....*
gi 564400362 518 QDIKRQLKVVERLLS 532
Cdd:cd04402  168 EDLKKVTSLVQFLIE 182
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
361-531 3.06e-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: 85.82  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKF-LKVKTVPLlskvDD--IHAICSLLKDFLRNLKEPLLTFWL 437
Cdd:cd04406   15 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLdTDANSVNL----DDynIHVIASVFKQWLRDLPNPLMTFEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 438 SKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAKIFGPTIVaHTVPNPDPVTM 516
Cdd:cd04406   91 YEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIAlQEETNRMSANALAIVFAPCIL-RCPDTTDPLQS 169
                        170
                 ....*....|....*
gi 564400362 517 FQDIKRQLKVVERLL 531
Cdd:cd04406  170 VQDISKTTTCVELIV 184
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
360-503 1.45e-17

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


Pssm-ID: 239856  Cd Length: 216  Bit Score: 82.01  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 360 MIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVK----ELKEKFLKVKTvpLLSKVdDIHAICSLLKDFLRNLKEPLLTF 435
Cdd:cd04391   21 KVPLIFQKLINKLEERGLETEGILRIPGSAQRVKflcqELEAKFYEGTF--LWDQV-KQHDAASLLKLFIRELPQPLLTV 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564400362 436 WLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRV-AQSPSTKMDVVNLAKIFGPTI 503
Cdd:cd04391   98 EYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVvDHEEKNKMNLWNVAMIMAPNL 166
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
361-547 2.59e-17

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: 80.87  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKT-VPLLSKVDDIHaICSLLKDFLRNLKEPLLTFWLSK 439
Cdd:cd04397   27 IPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTeVPDLSKENPVQ-LAALLKKFLRELPDPLLTFKLYR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 440 AFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVA------QSPSTKMDVVNLAKIFGPTIVahtVPNPDP 513
Cdd:cd04397  106 LWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSsfshidEETGSKMDIHNLATVITPNIL---YSKTDN 182
                        170       180       190
                 ....*....|....*....|....*....|....
gi 564400362 514 VTMFQDIKRQLKVVERLlslpLEYWNQFMMVEQE 547
Cdd:cd04397  183 PNTGDEYFLAIEAVNYL----IENNEEFCEVPDE 212
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
344-514 8.84e-16

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: 75.92  E-value: 8.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 344 KIGEGMLADFVSQTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTvPLLSKVD--DIHAICSLL 421
Cdd:cd04383    1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGED-PLADDQNdhDINSVAGVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 422 KDFLRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFG 500
Cdd:cd04383   80 KLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQfSDENMMDPYNLAICFG 159
                        170
                 ....*....|....*
gi 564400362 501 PTIVAhtVP-NPDPV 514
Cdd:cd04383  160 PTLMP--VPeGQDQV 172
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
361-531 9.91e-16

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: 75.89  E-value: 9.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEA-GLYRISGCDRTVKELKEKFLKVKtVPLlSKVDDIHAICSLLKDFLRNLKEPLltfwLSK 439
Cdd:cd04389   21 LPWILTFLSEKVLALGGFQTeGIFRVPGDIDEVNELKLRVDQWD-YPL-SGLEDPHVPASLLKLWLRELEEPL----IPD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 440 AFMEAAEITDEDnsTAAMYQAVSELPQANRDTLAFLMIHLQRVAQS---PSTKMDVVNLAKIFGPTIVAHTvpNPDPVTM 516
Cdd:cd04389   95 ALYQQCISASED--PDKAVEIVQKLPIINRLVLCYLINFLQVFAQPenvAHTKMDVSNLAMVFAPNILRCT--SDDPRVI 170
                        170
                 ....*....|....*
gi 564400362 517 FQDIKRQLKVVERLL 531
Cdd:cd04389  171 FENTRKEMSFLRTLI 185
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
361-505 5.65e-15

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: 74.05  E-value: 5.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEaGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDIHAicsLLKDFLRNLKEPLLTFWLSKA 440
Cdd:cd04394   20 VPKFLVDACTFLLDHLSTE-GLFRKSGSVVRQKELKAKLEGGEACLSSALPCDVAG---LLKQFFRELPEPLLPYDLHEA 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362 441 FMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTIVA 505
Cdd:cd04394   96 LLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQrCSENKMDSSNLAVIFAPNLFQ 161
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
361-506 1.43e-12

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: 67.44  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 361 IPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFlkvKTVPLLSKVDD-----IHAICSLLKDFLRNLKEPLLTF 435
Cdd:cd04396   32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIF---STPPDYGKSFDwdgytVHDAASVLRRYLNNLPEPLVPL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 436 WLSKAFME----------------AAEITDEDNSTAAMYQA-VSELPQANRDTLAFLMIHLQRVA-QSPSTKMDVVNLAK 497
Cdd:cd04396  109 DLYEEFRNplrkrprilqymkgriNEPLNTDIDQAIKEYRDlITRLPNLNRQLLLYLLDLLAVFArNSDKNLMTASNLAA 188

                 ....*....
gi 564400362 498 IFGPTIVAH 506
Cdd:cd04396  189 IFQPGILSH 197
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
286-334 8.20e-12

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: 60.22  E-value: 8.20e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd00029    1 HRFVPTTFSSPTFCDVCGKLIWgLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
374-504 3.26e-11

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: 63.25  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 374 QRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFWLSKAFMEAAEIT----- 448
Cdd:cd04392   21 EKNLRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLCqfdek 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564400362 449 -------DEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQSPST-KMDVVNLAKIFGPTIV 504
Cdd:cd04392  101 gnktsapDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKnKMSADNLALLFTPHLI 164
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
350-540 2.47e-09

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 57.58  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 350 LADFVSQTSP--MIPAIVVSCVNEIEQRGLTEAGLYRI-SGCDRTvkELKEKFLKVKTVPLLSKVDdIHAICSLLKDFLR 426
Cdd:cd04388    2 LPDLTEQFSPpdVAPPLLIKLVEAIEKKGLESSTLYRTqSSSSLT--ELRQILDCDAASVDLEQFD-VAALADALKRYLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 427 NLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSE---LPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPT 502
Cdd:cd04388   79 DLPNPVIPAPVYSEMISRAQEVQSSDEYAQLLRKLIRspnLPHQYWLTLQYLLKHFFRLCQsSSKNLLSARALAEIFSPL 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564400362 503 IVAHTVPNPDpvtmfqDIKRQLKVVERLLSlplEYWNQ 540
Cdd:cd04388  159 LFRFQPASSD------SPEFHIRIIEVLIT---SEWNE 187
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
286-334 8.50e-09

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: 51.96  E-value: 8.50e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564400362 286 HDFVSKTVIKPESCVPCGKRI--KFGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20831    6 HTFVATHFKGGPSCAVCNKLIpgRFGKQGYQCRDCGLICHKRCHVKVETHC 56
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
372-503 2.83e-08

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: 54.73  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 372 IEQRGLTEAGLYRISGCDRTVKELKEKflkVKTVPLLSKVDDIHA--ICSLLKDFLRNLKEPLLTFWLSKAFMEAAEITD 449
Cdd:cd04375   31 LRNNALDQVGLFRKSGVKSRIQKLRSM---IESSTDNVNYDGQQAydVADMLKQYFRDLPEPLLTNKLSETFIAIFQYVP 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564400362 450 EDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVAQ-SPSTKMDVVNLAKIFGPTI 503
Cdd:cd04375  108 KEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAPSL 162
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
286-334 7.32e-07

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: 46.31  E-value: 7.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564400362   286 HDFVSKTVIKPESCVPCGKRIKFG-KLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSfKQGLRCSECKVKCHKKCADKVPKAC 50
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
336-532 8.11e-07

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: 50.42  E-value: 8.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 336 PPLVGTPVKIGEGMLADFVSQTSPMIPAIVVSCVNEIEQRGLTEAGLYRISGcdrTVKELKEKFLKV------KTVPLLS 409
Cdd:cd04380   25 DPGIRNLIDQLELGDNPDYSEVPLSIPKEIWRLVDYLYTRGLAQEGLFEEPG---LPSEPGELLAEIrdaldtGSPFNSP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564400362 410 KvdDIHAICSLLKDFLRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQavseLPQANRDTLAFLMIHLQRVA-QSPST 488
Cdd:cd04380  102 G--SAESVAEALLLFLESLPDPIIPYSLYERLLEAVANNEEDKRQVIRIS----LPPVHRNVFVYLCSFLRELLsESADR 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564400362 489 KMDVVNLAKIFGPTIVAHTVPNPDPVTMfQDIKRQLKVVERLLS 532
Cdd:cd04380  176 GLDENTLATIFGRVLLRDPPRAGGKERR-AERDRKRAFIEQFLL 218
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
286-336 2.76e-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: 44.74  E-value: 2.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564400362  286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPCIP 336
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWgLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
286-334 6.14e-06

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. 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: 410364  Cd Length: 56  Bit Score: 43.77  E-value: 6.14e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20814    5 HRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTC 53
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
286-334 1.06e-05

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: 42.70  E-value: 1.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564400362 286 HDFVSKTVIkPESCVPCGKRIKFGklsLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20812    3 HRFSKKLFM-RQTCDYCHKQMFFG---LKCKDCKYKCHKKCAKKAPPSC 47
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
286-334 1.17e-05

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, 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. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is 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. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 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: 410358  Cd Length: 52  Bit Score: 42.71  E-value: 1.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20808    2 HNFQETTYFKPTFCDHCTGLLWgLIKQGYKCKDCGINCHKHCKDLVVVEC 51
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
285-338 1.82e-05

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: 42.57  E-value: 1.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564400362 285 LHDFVSKTVIKPESCVPCGKRIkfGKLSLKCRDCRLVSHPECRDRCPLPCIPPL 338
Cdd:cd20889    2 SHTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKVVTPCFPPV 53
C1_RASGRP2 cd20861
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 ...
285-334 1.87e-05

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: 42.57  E-value: 1.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564400362 285 LHDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20861    3 IHNFAERTFLRPVACRHCKNLIlGIYKQGLKCRACGVNCHKQCKDHLSIEC 53
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
283-331 1.33e-04

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. 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: 410375  Cd Length: 55  Bit Score: 39.95  E-value: 1.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564400362 283 MRLHDFVSKTVIKPESCVPCGKRIKFgKLSLKCRDCRLVSHPECRDRCP 331
Cdd:cd20825    1 EGKHDFVLTQFQNATYCDFCKKKIWL-KEAFQCRLCGMICHKKCLDKCQ 48
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
286-334 1.66e-04

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: 39.61  E-value: 1.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20824    2 HNFKPHSFSIPTKCDYCGEKIwGLSKKGLSCKDCGFNCHIKCELKVPPEC 51
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
286-334 2.14e-04

protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. 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: 410370  Cd Length: 52  Bit Score: 39.35  E-value: 2.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20820    2 HRFVPLELEQPTWCDLCGSVIlGLFRKCLRCANCKMTCHPRCRSLVCLTC 51
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
286-335 2.55e-04

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. 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: 410361  Cd Length: 49  Bit Score: 39.20  E-value: 2.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIKFGklsLKCRDCRLVSHPECRDRCPLPCI 335
Cdd:cd20811    3 HNFVRKTFFTLAFCDVCRKLLFQG---FRCQTCGFKFHQRCSDQVPALCE 49
C1_p190RhoGEF cd20876
protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange ...
279-335 3.24e-04

protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange factor (p190RhoGEF) and similar proteins; p190RhoGEF, also called Rho guanine nucleotide exchange factor (RGNEF), Rho guanine nucleotide exchange factor 28 (ARHGEF28), or RIP2, is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. In addition to the Dbl homology (DH)-PH domain, p190RhoGEF contains an N-terminal C1 (Protein kinase C conserved region 1) 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: 410426  Cd Length: 61  Bit Score: 38.96  E-value: 3.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564400362 279 QNNGmrlHDFVSKTVIKPESCVPCGKRIkFGKLSLKCRDCRLVSHPECRDRCPlPCI 335
Cdd:cd20876    4 QSNG---HQFVTGSFSGPTLCVVCDKPV-TGKELLQCSNCTVNVHKGCKESAP-PCT 55
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
286-334 3.91e-04

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. 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: 410436  Cd Length: 50  Bit Score: 38.52  E-value: 3.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 564400362 286 HDFVSkTVIKPESCVPCGKRIkFGKlSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20886    4 HRFEP-GALGPGWCDLCGRYI-LSQ-ALRCTNCKYTCHSECRDLVQLDC 49
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
286-337 4.85e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; 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. It contains 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 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: 410437  Cd Length: 53  Bit Score: 38.22  E-value: 4.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564400362 286 HDFVSKTVIKPESCVPCgkRIKFGKLSLKCRDCRLVSHPECRDRCPLPCIPP 337
Cdd:cd20887    3 HSFKEKTFKKKRACAVC--REPVGGQGLVCRVCKVASHKKCEAKVTSACQPP 52
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
286-337 7.90e-04

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: 37.75  E-value: 7.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKlslKCRDCRLVSHPECRDRCPLPCIPP 337
Cdd:cd20826    3 HSFKEKSFRKPRTCDVCKQIIWnEGS---SCRVCKYACHRKCEPKVTAACSPS 52
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
286-335 8.62e-04

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: 38.84  E-value: 8.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPCI 335
Cdd:cd20842   35 HTFVIHSYTRPTVCQYCKKLLKgLFRQGLQCKDCKFNCHKRCAPKVPNNCL 85
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
286-334 1.30e-03

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. 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: 410435  Cd Length: 54  Bit Score: 37.25  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20885    4 HDFQPCSLTNPTWCDLCGDFIwGLYKQCLRCTHCKYTCHLRCRDLVTLDC 53
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
286-335 1.47e-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: 37.65  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPCI 335
Cdd:cd20843   12 HTFVIHSYTRPTVCQFCKKLLKgLFRQGLQCKDCKFNCHKRCATRVPNDCL 62
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
286-346 1.51e-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: 37.68  E-value: 1.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPCIPPLV--GTPVKIG 346
Cdd:cd20844    6 HTFAVHSYTRPTICQYCKRLLKgLFRQGMQCKDCRFNCHKRCASKVPRDCLGEVTfnGEPASPG 69
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
286-334 1.73e-03

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. 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: 410367  Cd Length: 51  Bit Score: 36.92  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPlPC 334
Cdd:cd20817    1 HSFQEHTFKKPTFCDVCKELLVgLSKQGLRCKNCKMNVHHKCQEGVP-DC 49
C1_p190RhoGEF-like cd20815
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...
286-335 2.03e-03

protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide exchange factor (p190RhoGEF)-like family; The p190RhoGEF-like protein family includes p190RhoGEF, Rho guanine nucleotide exchange factor 2 (ARHGEF2), A-kinase anchor protein 13 (AKAP-13) and similar proteins. p190RhoGEF is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. ARHGEF2 acts as a guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. AKAP-13 is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. It activates RhoA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Members of this family share a common domain architecture containing C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains. Some members may contain additional domains such as the DUF5401 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: 410365  Cd Length: 54  Bit Score: 36.63  E-value: 2.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIKfGKLSLKCRDCRLVSH-PECRDRCPlPCI 335
Cdd:cd20815    4 HQFVPVSFSNSTKCDVCSKPLT-NKPALQCENCSVNVHdSSCKDQLA-DCT 52
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
286-334 2.84e-03

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: 36.11  E-value: 2.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20796    2 HTFVVHTYTKPTVCQHCKKLLKgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
43-108 2.87e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 39.63  E-value: 2.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362   43 KKCQRTNQELEKFKDLLLKAETgrsaldvKLKHARnqvdveiKRRQRAEAECAKLEQQIQLIRDIL 108
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMK-------KLEEAE-------KRAEKAEAEVAALNRRIQLLEEEL 52
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
282-337 2.99e-03

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: 36.39  E-value: 2.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564400362 282 GMRLHDFVSKTVIKPESCVPCGKRIKfgKLSLKCRDCRLVSHPECRDRCPLPCIPP 337
Cdd:cd20888    2 APHTHTFKVKTFKKVKSCGICKQAIT--REGSTCRVCKLSCHKKCEAKVATPCVPA 55
C1_DGKtheta_typeV_rpt2 cd20804
second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
286-328 4.82e-03

second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three 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: 410354  Cd Length: 57  Bit Score: 35.74  E-value: 4.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIkFGKLSLKCRDCRLVSHPECRD 328
Cdd:cd20804    6 HCWSEPGHSKRKFCNVCRKRL-EDSPAFRCEVCEYYVHSDCQD 47
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
285-334 7.03e-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: 35.29  E-value: 7.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564400362 285 LHDFVSKTVIKPESCVPCGKRIkFG--KLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20860    2 PHNFQETTYLKPTFCDNCAGFL-WGviKQGYRCKDCGMNCHKQCKDLVVFEC 52
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
286-334 7.61e-03

second 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 domain. 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 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: 410343  Cd Length: 50  Bit Score: 34.95  E-value: 7.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564400362 286 HDFVSKTVIKPESCVPCGKRIkFG--KLSLKCRDCRLVSHPECRDRCPLPC 334
Cdd:cd20793    1 HKFKVHTYYSPTFCDHCGSLL-YGlvRQGLKCKDCGMNVHHRCKENVPHLC 50
 
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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