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Conserved domains on  [gi|21361397|ref|NP_037409|]
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rac GTPase-activating protein 1 isoform a [Homo sapiens]

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 ...
346-539 2.58e-126

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: 370.47  E-value: 2.58e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 346 IGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDdIHAICSLLKDF 425
Cdd:cd04382   1 IGTGELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVD-IHVICGCLKDF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 426 LRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHTKMDVANLAKVFGPTIV 505
Cdd:cd04382  80 LRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTIV 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 21361397 506 AHAVPNPDPVTMLQDIKRQPKVVERLLSLPLEYW 539
Cdd:cd04382 160 GYSVPNPDPMTILQDTVRQPRVVERLLEIPSDYW 193
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
285-338 2.23e-28

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: 107.49  E-value: 2.23e-28
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21361397 285 RLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPT 338
Cdd:cd20821   1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPT 54
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
13-105 2.34e-03

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397     13 EQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVK---LKHARNQVDVEIKRRQR- 88
Cdd:TIGR02168  210 EKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQKe 289
                           90       100
                   ....*....|....*....|
gi 21361397     89 ---AEADCEKLERQIQLIRE 105
Cdd:TIGR02168  290 lyaLANEISRLEQQKQILRE 309
 
Name Accession Description Interval E-value
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
346-539 2.58e-126

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: 370.47  E-value: 2.58e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 346 IGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDdIHAICSLLKDF 425
Cdd:cd04382   1 IGTGELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVD-IHVICGCLKDF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 426 LRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHTKMDVANLAKVFGPTIV 505
Cdd:cd04382  80 LRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTIV 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 21361397 506 AHAVPNPDPVTMLQDIKRQPKVVERLLSLPLEYW 539
Cdd:cd04382 160 GYSVPNPDPMTILQDTVRQPRVVERLLEIPSDYW 193
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
363-507 1.84e-55

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.06  E-value: 1.84e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397   363 PSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNRAF 442
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361397   443 MEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPH-TKMDVANLAKVFGPTIVAH 507
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDvNKMNAHNLAIVFGPTLLRP 146
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
360-533 6.82e-50

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: 170.91  E-value: 6.82e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397    360 PMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLR-VKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFRL 438
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYD-VHDVAGLLKLFLRELPEPLITYEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397    439 NRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVAhavPNPDPVTM 517
Cdd:smart00324  80 YEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTLLR---PPDGEVAS 156
                          170
                   ....*....|....*.
gi 21361397    518 LQDIKRQPKVVERLLS 533
Cdd:smart00324 157 LKDIRHQNTVIEFLIE 172
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
285-338 2.23e-28

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: 107.49  E-value: 2.23e-28
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21361397 285 RLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPT 338
Cdd:cd20821   1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPT 54
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
287-335 2.05e-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: 47.85  E-value: 2.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 21361397    287 HDFVSKTVIKPESCVPCGKRIKFG-KLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSfKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
287-337 6.82e-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: 43.58  E-value: 6.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21361397   287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPCIP 337
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWgLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
13-105 2.34e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397     13 EQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVK---LKHARNQVDVEIKRRQR- 88
Cdd:TIGR02168  210 EKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQKe 289
                           90       100
                   ....*....|....*....|
gi 21361397     89 ---AEADCEKLERQIQLIRE 105
Cdd:TIGR02168  290 lyaLANEISRLEQQKQILRE 309
 
Name Accession Description Interval E-value
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
346-539 2.58e-126

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: 370.47  E-value: 2.58e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 346 IGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDdIHAICSLLKDF 425
Cdd:cd04382   1 IGTGELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVD-IHVICGCLKDF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 426 LRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHTKMDVANLAKVFGPTIV 505
Cdd:cd04382  80 LRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTIV 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 21361397 506 AHAVPNPDPVTMLQDIKRQPKVVERLLSLPLEYW 539
Cdd:cd04382 160 GYSVPNPDPMTILQDTVRQPRVVERLLEIPSDYW 193
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
363-507 1.84e-55

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.06  E-value: 1.84e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397   363 PSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNRAF 442
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361397   443 MEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPH-TKMDVANLAKVFGPTIVAH 507
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDvNKMNAHNLAIVFGPTLLRP 146
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
360-533 6.82e-50

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: 170.91  E-value: 6.82e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397    360 PMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLR-VKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFRL 438
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYD-VHDVAGLLKLFLRELPEPLITYEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397    439 NRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVAhavPNPDPVTM 517
Cdd:smart00324  80 YEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTLLR---PPDGEVAS 156
                          170
                   ....*....|....*.
gi 21361397    518 LQDIKRQPKVVERLLS 533
Cdd:smart00324 157 LKDIRHQNTVIEFLIE 172
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
363-533 7.07e-48

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 165.55  E-value: 7.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 363 PSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFRLNRAF 442
Cdd:cd00159   1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYD-VHDVASLLKLYLRELPEPLIPFELYDEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 443 MEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVahaVPNPDPVTMLQDI 521
Cdd:cd00159  80 IELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQnSEVNKMTASNLAIVFAPTLL---RPPDSDDELLEDI 156
                       170
                ....*....|..
gi 21361397 522 KRQPKVVERLLS 533
Cdd:cd00159 157 KKLNEIVEFLIE 168
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
361-532 1.39e-38

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: 141.00  E-value: 1.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 361 MIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLR-VKTVPLLSKVD---DIHAICSLLKDFLRNLKEPLLTF 436
Cdd:cd04398  15 NVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKdPLNVLLISPEDyesDIHSVASLLKLFFRELPEPLLTK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 437 RLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVahavpnPDPV 515
Cdd:cd04398  95 ALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEhESVNRMSVNNLAIIWGPTLM------NAAP 168
                       170
                ....*....|....*..
gi 21361397 516 TMLQDIKRQPKVVERLL 532
Cdd:cd04398 169 DNAADMSFQSRVIETLL 185
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
356-532 5.59e-36

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: 133.68  E-value: 5.59e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 356 SQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLR-VKTVPLLS-KVDDIHAICSLLKDFLRNLKEPL 433
Cdd:cd04395  12 SSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRgGFDIDLQDpRWRDVNVVSSLLKSFFRKLPEPL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 434 LTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVahAVPNP 512
Cdd:cd04395  92 FTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADnSEVNKMEPRNLAIVFGPTLV--RTSDD 169
                       170       180
                ....*....|....*....|
gi 21361397 513 DPVTMLQDIKRQPKVVERLL 532
Cdd:cd04395 170 NMETMVTHMPDQCKIVETLI 189
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
362-533 1.77e-33

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: 126.86  E-value: 1.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLR--VKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLN 439
Cdd:cd04372  16 RPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdgEKADISATVYPDINVITGALKLYFRDLPIPVITYDTY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 440 RAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVahAVPNPDPVTML 518
Cdd:cd04372  96 PKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLhEKDNKMNAENLGIVFGPTLM--RPPEDSALTTL 173
                       170
                ....*....|....*
gi 21361397 519 QDIKRQPKVVERLLS 533
Cdd:cd04372 174 NDMRYQILIVQLLIT 188
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
364-533 1.14e-31

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: 122.12  E-value: 1.14e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 364 SIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKT-----VPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRL 438
Cdd:cd04374  30 KFVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGLDPKTstpgdVDLDNSEWEIKTITSALKTYLRNLPEPLMTYEL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 439 NRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTIVAhavPNPDPVTM 517
Cdd:cd04374 110 HNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSdHSKKNLMTVSNLGVVFGPTLLR---PQEETVAA 186
                       170
                ....*....|....*.
gi 21361397 518 LQDIKRQPKVVERLLS 533
Cdd:cd04374 187 IMDIKFQNIVVEILIE 202
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
351-532 2.97e-31

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


Pssm-ID: 239842  Cd Length: 186  Bit Score: 120.24  E-value: 2.97e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 351 LADFVSQTSPmIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKflrVKTVPLLSKVDD--IHAICSLLKDFLRN 428
Cdd:cd04377   5 LSSLTSEDRS-VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQG---LDTDPDSVNLEDypIHVITSVLKQWLRE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 429 LKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTIVaH 507
Cdd:cd04377  81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVAlQEEVNRMSANALAIVFAPCIL-R 159
                       170       180
                ....*....|....*....|....*
gi 21361397 508 AVPNPDPVTMLQDIKRQPKVVERLL 532
Cdd:cd04377 160 CPDTADPLQSLQDVSKTTTCVETLI 184
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
362-504 5.17e-31

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: 119.34  E-value: 5.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLR-VKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNR 440
Cdd:cd04385  15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKdARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHA 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361397 441 AFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTI 504
Cdd:cd04385  95 EWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQkHSDENQMSVHNLALVFGPTL 159
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
362-533 1.50e-30

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: 118.68  E-value: 1.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDiHAICSLLKDFLRNLKEPLLTFRLNRA 441
Cdd:cd04378  16 VPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSP-HDISSVLKLFLRQLPEPLILFRLYND 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 442 FMEAAEITDEDNS--------------IAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTIVa 506
Cdd:cd04378  95 FIALAKEIQRDTEedkapntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAeQFEENKMSPNNLGIVFGPTLI- 173
                       170       180
                ....*....|....*....|....*....
gi 21361397 507 HAVPNPDPVTM--LQDIKRQPKVVERLLS 533
Cdd:cd04378 174 RPRPGDADVSLssLVDYGYQARLVEFLIT 202
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
362-533 3.56e-29

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: 114.41  E-value: 3.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPL-LSKVDDIHAICSLLKDFLRNLKEPLLTFRLNR 440
Cdd:cd04403  16 VPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLdDSKWEDIHVITGALKLFFRELPEPLFPYSLFN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 441 AFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVAHAVPNPDP-VTML 518
Cdd:cd04403  96 DFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEhGEKNRMTTQNLAIVFGPTLLRPEQETGNIaVHMV 175
                       170
                ....*....|....*
gi 21361397 519 QdikrQPKVVERLLS 533
Cdd:cd04403 176 Y----QNQIVELILL 186
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
357-534 1.39e-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: 113.10  E-value: 1.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 357 QTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKF-LRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLT 435
Cdd:cd04387  11 RERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFdTNNKDVSVMLSEMDVNAIAGTLKLYFRELPEPLFT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 436 FRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVAHAVPNPDP 514
Cdd:cd04387  91 DELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAErEEVNKMSLHNLATVFGPTLLRPSEKESKI 170
                       170       180
                ....*....|....*....|
gi 21361397 515 VTMLQDIKRQPKVVERLLSL 534
Cdd:cd04387 171 PTNTMTDSWSLEVMSQVQVL 190
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
285-338 2.23e-28

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: 107.49  E-value: 2.23e-28
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21361397 285 RLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPT 338
Cdd:cd20821   1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPT 54
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
351-532 1.44e-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: 1.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 351 LADFVSQTSPmIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKflrVKTVPLLSKVDD--IHAICSLLKDFLRN 428
Cdd:cd04407   5 VGSLTSNKTS-VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQL---LQADPENVKLENypIHAITGLLKQWLRE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 429 LKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHT-KMDVANLAKVFGPTIVaH 507
Cdd:cd04407  81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVnRMSPNALAIVFAPCLL-R 159
                       170       180
                ....*....|....*....|....*
gi 21361397 508 AVPNPDPVTMLQDIKRQPKVVERLL 532
Cdd:cd04407 160 CPDSSDPLTSMKDVAKTTTCVEMLI 184
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
362-533 5.42e-26

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: 105.67  E-value: 5.42e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDiHAICSLLKDFLRNLKEPLLTFRLNRA 441
Cdd:cd04408  16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSP-HDITSVLKHFLKELPEPVLPFQLYDD 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 442 FMEAAEITDED------------NSIAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTIVaHA 508
Cdd:cd04408  95 FIALAKELQRDsekaaespsiveNIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAeRFEDNKMSPNNLGIVFGPTLL-RP 173
                       170       180
                ....*....|....*....|....*.
gi 21361397 509 VPNPD-PVTMLQDIKRQPKVVERLLS 533
Cdd:cd04408 174 LVGGDvSMICLLDTGYQAQLVEFLIS 199
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
341-504 3.77e-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: 3.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 341 GTPvkigegmLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKfLRVKTV--PLLSKVDDIHAI 418
Cdd:cd04386   6 GTP-------LEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAA-LDAGTFslPLDEFYSDPHAV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 419 CSLLKDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLA 497
Cdd:cd04386  78 ASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQkSDENKMSPSNIA 157

                ....*..
gi 21361397 498 KVFGPTI 504
Cdd:cd04386 158 IVLAPNL 164
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
360-504 9.08e-24

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


Pssm-ID: 239841  Cd Length: 206  Bit Score: 99.44  E-value: 9.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 360 PMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVdDIHAICSLLKDFLRNLKEPLLTFRLN 439
Cdd:cd04376   7 RQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENH-SVHDVAALLKEFFRDMPDPLLPRELY 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361397 440 RAFMEAAEITDEDNsIAAMYQAVGELPQANRDTLAFLMIHLQRVAQS------------PHTKMDVANLAKVFGPTI 504
Cdd:cd04376  86 TAFIGTALLEPDEQ-LEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHaadsidedgqevSGNKMTSLNLATIFGPNL 161
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
351-517 1.26e-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: 98.30  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 351 LADFVSQTSPmIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICSLLKDFLRNLK 430
Cdd:cd04373   5 LANVVTSEKP-IPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFSELP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 431 EPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVahav 509
Cdd:cd04373  84 DPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQnSKVNLMTSENLSICFWPTLM---- 159

                ....*...
gi 21361397 510 pNPDPVTM 517
Cdd:cd04373 160 -RPDFTSM 166
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
357-513 2.91e-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: 97.53  E-value: 2.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 357 QTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPlLSKVDDIHAICSLLKDFLRNLKEPLLTF 436
Cdd:cd04393  15 QPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVD-LSKEADVCSAASLLRLFLQELPEGLIPA 93
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361397 437 RLNRAFMEA-AEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTIVaHAVPNPD 513
Cdd:cd04393  94 SLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVAsQHHENRMTAENLAAVFGPDVF-HVYTDVE 171
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
362-520 4.59e-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: 97.04  E-value: 4.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIE-QRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLL--SKVDDIHAICSLLKDFLRNLKEPLLTFRL 438
Cdd:cd04400  22 LPSVVYRCIEYLDkNRAIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFssSLYPDVHTVAGLLKLYLRELPTLILGGEL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 439 NRAFMEAAEI-TDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRV-AQSPHTKMDVANLAKVFGPTIvahAVPNPDPVT 516
Cdd:cd04400 102 HNDFKRLVEEnHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIiEHSDVNKMNLRNVCIVFSPTL---NIPAGIFVL 178

                ....
gi 21361397 517 MLQD 520
Cdd:cd04400 179 FLTD 182
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
361-505 5.32e-23

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 97.02  E-value: 5.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 361 MIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLlSKVDDIHAICSLLKDFLRNLKEPLLTFRLnr 440
Cdd:cd04404  22 PIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDF-DQYEDVHLPAVILKTFLRELPEPLLTFDL-- 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361397 441 aFMEAAEIT--DEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIV 505
Cdd:cd04404  99 -YDDIVGFLnvDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAhSDQNKMTNSNLAVVFGPNLL 165
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
362-504 6.85e-23

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


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 96.35  E-value: 6.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRvKTVPLLSKVDdIHAICSLLKDFLRNLKEPLLTFRLNRA 441
Cdd:cd04381  20 LPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNR-RESPNLEEYE-PPTVASLLKQYLRELPEPLLTKELMPR 97
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361397 442 FMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHL-QRVAQSPHTKMDVANLAKVFGPTI 504
Cdd:cd04381  98 FEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMdHVIAQELETKMNIQNISIVLSPTV 161
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
361-519 2.06e-22

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: 95.20  E-value: 2.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 361 MIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTvPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNR 440
Cdd:cd04390  21 LVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGER-PSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 441 AFMEAAEITDEDNSIA--AMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVAHAVpnPDPVTM 517
Cdd:cd04390 100 DFLSCAQLLSKDEEKGlgELMKQVSILPKVNYNLLSYICRFLDEVQSnSSVNKMSVQNLATVFGPNILRPKV--EDPATI 177

                ..
gi 21361397 518 LQ 519
Cdd:cd04390 178 ME 179
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
352-532 4.73e-22

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: 94.87  E-value: 4.73e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 352 ADF--VSQTSP-MIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDiHAICSLLKDFLRN 428
Cdd:cd04409   3 ADFaqVAKKSPdGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSP-HDISNVLKLYLRQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 429 LKEPLLTFRLNRAFM----EAAEITDEDNS------------------IAAMYQAVGELPQANRDTLAFLMIHLQRVA-Q 485
Cdd:cd04409  82 LPEPLILFRLYNEFIglakESQHVNETQEAkknsdkkwpnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRVSeQ 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21361397 486 SPHTKMDVANLAKVFGPTIVaHAVPNPDPVTM--LQDIKRQPKVVERLL 532
Cdd:cd04409 162 AEENKMSASNLGIIFGPTLI-RPRPTDATVSLssLVDYPHQARLVELLI 209
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
351-504 5.97e-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: 94.11  E-value: 5.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 351 LADFVSQTSPMIPSIVVHCVNEIEQRGLTeTGLYRISGCDRTVKELKEKFlRVKTVPLLSK---VDDIHAICSLLKDFLR 427
Cdd:cd04384   7 LTEHLLNSGQDVPQVLKSCTEFIEKHGIV-DGIYRLSGIASNIQRLRHEF-DSEQIPDLTKdvyIQDIHSVSSLCKLYFR 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361397 428 NLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQS-PHTKMDVANLAKVFGPTI 504
Cdd:cd04384  85 ELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYcSITNMHAKNLAIVWAPNL 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
358-507 6.79e-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: 94.07  E-value: 6.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 358 TSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSK--VDDIHAICSLLKDFLRNLKEPLLT 435
Cdd:cd04379  14 ESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEelYPDINVITGVLKDYLRELPEPLIT 93
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361397 436 FRLNRAFMEAAEI---TDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTIVAH 507
Cdd:cd04379  94 PQLYEMVLEALAValpNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLsNSERNKMTPQNLAVCFGPVLMFC 169
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
361-533 1.77e-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: 89.67  E-value: 1.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 361 MIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLlsKVDDIHAICSLLKDFLRNLKEPLLTFRLNR 440
Cdd:cd04402  14 NLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDL--KAEPVLLLASVLKDFLRNIPGSLLSSDLYE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 441 AFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHT-KMDVANLAKVFGPTIVAhavpNPDPVTML- 518
Cdd:cd04402  92 EWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETnKMDAFNLAVCIAPSLLW----PPASSELQn 167
                       170
                ....*....|....*
gi 21361397 519 QDIKRQPKVVERLLS 533
Cdd:cd04402 168 EDLKKVTSLVQFLIE 182
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
362-532 2.98e-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: 2.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKF-LRVKTVPLlskvDD--IHAICSLLKDFLRNLKEPLLTFRL 438
Cdd:cd04406  15 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLdTDANSVNL----DDynIHVIASVFKQWLRDLPNPLMTFEL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 439 NRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAKVFGPTIVaHAVPNPDPVTM 517
Cdd:cd04406  91 YEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIAlQEETNRMSANALAIVFAPCIL-RCPDTTDPLQS 169
                       170
                ....*....|....*
gi 21361397 518 LQDIKRQPKVVERLL 532
Cdd:cd04406 170 VQDISKTTTCVELIV 184
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
362-504 5.59e-18

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 82.80  E-value: 5.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKT-VPLLSKVDDIHaICSLLKDFLRNLKEPLLTFRLNR 440
Cdd:cd04397  27 IPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTeVPDLSKENPVQ-LAALLKKFLRELPDPLLTFKLYR 105
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 441 AFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPH------TKMDVANLAKVFGPTI 504
Cdd:cd04397 106 LWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHideetgSKMDIHNLATVITPNI 175
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
362-532 7.04e-17

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 78.97  E-value: 7.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTET-GLYRISGCDRTVKELKEKFLRVKtVPLlSKVDDIHAICSLLKDFLRNLKEPLLTFRLNR 440
Cdd:cd04389  21 LPWILTFLSEKVLALGGFQTeGIFRVPGDIDEVNELKLRVDQWD-YPL-SGLEDPHVPASLLKLWLRELEEPLIPDALYQ 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 441 AFMEAAEitDEDNSIAAmyqaVGELPQANRDTLAFLMIHLQRVAQS---PHTKMDVANLAKVFGPTIVahAVPNPDPVTM 517
Cdd:cd04389  99 QCISASE--DPDKAVEI----VQKLPIINRLVLCYLINFLQVFAQPenvAHTKMDVSNLAMVFAPNIL--RCTSDDPRVI 170
                       170
                ....*....|....*
gi 21361397 518 LQDIKRQPKVVERLL 532
Cdd:cd04389 171 FENTRKEMSFLRTLI 185
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
361-519 2.48e-16

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: 78.16  E-value: 2.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 361 MIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVK----ELKEKFLRVKTvpLLSKVdDIHAICSLLKDFLRNLKEPLLTF 436
Cdd:cd04391  21 KVPLIFQKLINKLEERGLETEGILRIPGSAQRVKflcqELEAKFYEGTF--LWDQV-KQHDAASLLKLFIRELPQPLLTV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 437 RLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRV-AQSPHTKMDVANLAKVFGPTIVAHAVPNPDPV 515
Cdd:cd04391  98 EYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVvDHEEKNKMNLWNVAMIMAPNLFPPRGKHSKDN 177

                ....
gi 21361397 516 TMLQ 519
Cdd:cd04391 178 ESLQ 181
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
362-506 5.25e-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: 5.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTEtGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAicsLLKDFLRNLKEPLLTFRLNRA 441
Cdd:cd04394  20 VPKFLVDACTFLLDHLSTE-GLFRKSGSVVRQKELKAKLEGGEACLSSALPCDVAG---LLKQFFRELPEPLLPYDLHEA 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361397 442 FMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTIVA 506
Cdd:cd04394  96 LLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQrCSENKMDSSNLAVIFAPNLFQ 161
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
345-521 1.79e-14

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: 72.07  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 345 KIGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTvPLLSKVD--DIHAICSLL 422
Cdd:cd04383   1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGED-PLADDQNdhDINSVAGVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 423 KDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFG 501
Cdd:cd04383  80 KLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQfSDENMMDPYNLAICFG 159
                       170       180
                ....*....|....*....|.
gi 21361397 502 PTIVahAVP-NPDPVTMLQDI 521
Cdd:cd04383 160 PTLM--PVPeGQDQVSCQAHV 178
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
362-507 1.71e-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: 67.05  E-value: 1.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 362 IPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFlrvKTVPLLSKVDD-----IHAICSLLKDFLRNLKEPLLTF 436
Cdd:cd04396  32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIF---STPPDYGKSFDwdgytVHDAASVLRRYLNNLPEPLVPL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 437 RLNRAFME---------------AAEITDEDNSIA-AMYQA-VGELPQANRDTLAFLMIHLQRVA-QSPHTKMDVANLAK 498
Cdd:cd04396 109 DLYEEFRNplrkrprilqymkgrINEPLNTDIDQAiKEYRDlITRLPNLNRQLLLYLLDLLAVFArNSDKNLMTASNLAA 188

                ....*....
gi 21361397 499 VFGPTIVAH 507
Cdd:cd04396 189 IFQPGILSH 197
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
287-335 1.79e-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: 62.15  E-value: 1.79e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd00029   1 HRFVPTTFSSPTFCDVCGKLIWgLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
375-505 7.18e-12

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: 65.18  E-value: 7.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 375 QRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNRAFMEAAEIT----- 449
Cdd:cd04392  21 EKNLRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLCqfdek 100
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361397 450 -------DEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHT-KMDVANLAKVFGPTIV 505
Cdd:cd04392 101 gnktsapDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKnKMSADNLALLFTPHLI 164
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
373-504 1.44e-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: 55.50  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 373 IEQRGLTETGLYRISGCDRTVKELKEKflrVKTVPLLSKVDDIHA--ICSLLKDFLRNLKEPLLTFRLNRAFMEAAEITD 450
Cdd:cd04375  31 LRNNALDQVGLFRKSGVKSRIQKLRSM---IESSTDNVNYDGQQAydVADMLKQYFRDLPEPLLTNKLSETFIAIFQYVP 107
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21361397 451 EDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVFGPTI 504
Cdd:cd04375 108 KEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAPSL 162
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
351-513 3.96e-08

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: 53.72  E-value: 3.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 351 LADFVSQTSP--MIPSIVVHCVNEIEQRGLTETGLYRisgcDRTVKELKEkfLRVKTVPLLSKVD----DIHAICSLLKD 424
Cdd:cd04388   2 LPDLTEQFSPpdVAPPLLIKLVEAIEKKGLESSTLYR----TQSSSSLTE--LRQILDCDAASVDleqfDVAALADALKR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 425 FLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGE---LPQANRDTLAFLMIHLQRVAQ-SPHTKMDVANLAKVF 500
Cdd:cd04388  76 YLLDLPNPVIPAPVYSEMISRAQEVQSSDEYAQLLRKLIRspnLPHQYWLTLQYLLKHFFRLCQsSSKNLLSARALAEIF 155
                       170
                ....*....|...
gi 21361397 501 GPTIVAHAVPNPD 513
Cdd:cd04388 156 SPLLFRFQPASSD 168
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
287-335 4.76e-08

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: 49.65  E-value: 4.76e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361397 287 HDFVSKTVIKPESCVPCGKRI--KFGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20831   6 HTFVATHFKGGPSCAVCNKLIpgRFGKQGYQCRDCGLICHKRCHVKVETHC 56
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
287-335 2.05e-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: 47.85  E-value: 2.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 21361397    287 HDFVSKTVIKPESCVPCGKRIKFG-KLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSfKQGLRCSECKVKCHKKCADKVPKAC 50
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
287-335 1.48e-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: 45.70  E-value: 1.48e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20814   5 HRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTC 53
C1_RASGRP2 cd20861
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 ...
286-335 3.82e-06

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: 44.49  E-value: 3.82e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361397 286 LHDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20861   3 IHNFAERTFLRPVACRHCKNLIlGIYKQGLKCRACGVNCHKQCKDHLSIEC 53
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
287-335 5.76e-06

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: 43.47  E-value: 5.76e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21361397 287 HDFVSKTVIkPESCVPCGKRIKFGklsLKCRDCRVVSHPECRDRCPLPC 335
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 ...
287-335 6.48e-06

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: 43.48  E-value: 6.48e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20808   2 HNFQETTYFKPTFCDHCTGLLWgLIKQGYKCKDCGINCHKHCKDLVVVEC 51
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
287-337 6.82e-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: 43.58  E-value: 6.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21361397   287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPCIP 337
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWgLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
C1_p190RhoGEF cd20876
protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange ...
279-336 2.28e-05

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: 42.42  E-value: 2.28e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21361397 279 QSNGgmrlHDFVSKTVIKPESCVPCGKRIkFGKLSLKCRDCRVVSHPECRDRCPlPCI 336
Cdd:cd20876   4 QSNG----HQFVTGSFSGPTLCVVCDKPV-TGKELLQCSNCTVNVHKGCKESAP-PCT 55
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
339-533 4.64e-05

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: 45.02  E-value: 4.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 339 LIGTPVKIGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGcdrTVKELKEKFLRV------KTVPLLSKv 412
Cdd:cd04380  27 GIRNLIDQLELGDNPDYSEVPLSIPKEIWRLVDYLYTRGLAQEGLFEEPG---LPSEPGELLAEIrdaldtGSPFNSPG- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397 413 dDIHAICSLLKDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQavgeLPQANRDTLAFLMIHLQRVA-QSPHTKM 491
Cdd:cd04380 103 -SAESVAEALLLFLESLPDPIIPYSLYERLLEAVANNEEDKRQVIRIS----LPPVHRNVFVYLCSFLRELLsESADRGL 177
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21361397 492 DVANLAKVFGPTIVAHAVPNPDPVTMlQDIKRQPKVVERLLS 533
Cdd:cd04380 178 DENTLATIFGRVLLRDPPRAGGKERR-AERDRKRAFIEQFLL 218
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
286-337 7.26e-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: 40.64  E-value: 7.26e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21361397 286 LHDFVSKTVIKPESCVPCGKRIkfGKLSLKCRDCRVVSHPECRDRCPLPCIP 337
Cdd:cd20889   2 SHTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKVVTPCFP 51
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
287-336 8.72e-05

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: 40.36  E-value: 8.72e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIKFGklsLKCRDCRVVSHPECRDRCPLPCI 336
Cdd:cd20811   3 HNFVRKTFFTLAFCDVCRKLLFQG---FRCQTCGFKFHQRCSDQVPALCE 49
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
287-335 1.57e-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: 1.57e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20824   2 HNFKPHSFSIPTKCDYCGEKIwGLSKKGLSCKDCGFNCHIKCELKVPPEC 51
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
287-335 2.22e-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: 2.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20820   2 HRFVPLELEQPTWCDLCGSVIlGLFRKCLRCANCKMTCHPRCRSLVCLTC 51
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
284-332 2.22e-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: 39.18  E-value: 2.22e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21361397 284 MRLHDFVSKTVIKPESCVPCGKRIKFgKLSLKCRDCRVVSHPECRDRCP 332
Cdd:cd20825   1 EGKHDFVLTQFQNATYCDFCKKKIWL-KEAFQCRLCGMICHKKCLDKCQ 48
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
287-335 4.31e-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: 4.31e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21361397 287 HDFVSkTVIKPESCVPCGKRIkFGKlSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20886   4 HRFEP-GALGPGWCDLCGRYI-LSQ-ALRCTNCKYTCHSECRDLVQLDC 49
C1_p190RhoGEF-like cd20815
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...
287-336 4.41e-04

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: 38.56  E-value: 4.41e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIKfGKLSLKCRDCRVVSH-PECRDRCPlPCI 336
Cdd:cd20815   4 HQFVPVSFSNSTKCDVCSKPLT-NKPALQCENCSVNVHdSSCKDQLA-DCT 52
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
287-337 5.74e-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: 5.74e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361397 287 HDFVSKTVIKPESCVPCgkRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIP 337
Cdd:cd20887   3 HSFKEKTFKKKRACAVC--REPVGGQGLVCRVCKVASHKKCEAKVTSACQP 51
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
287-338 7.30e-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: 7.30e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKlslKCRDCRVVSHPECRDRCPLPCIPT 338
Cdd:cd20826   3 HSFKEKSFRKPRTCDVCKQIIWnEGS---SCRVCKYACHRKCEPKVTAACSPS 52
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
287-335 9.32e-04

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: 37.69  E-value: 9.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPlPC 335
Cdd:cd20817   1 HSFQEHTFKKPTFCDVCKELLVgLSKQGLRCKNCKMNVHHKCQEGVP-DC 49
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
287-336 1.08e-03

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


Pssm-ID: 410392  Cd Length: 94  Bit Score: 38.84  E-value: 1.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPCI 336
Cdd:cd20842  35 HTFVIHSYTRPTVCQYCKKLLKgLFRQGLQCKDCKFNCHKRCAPKVPNNCL 85
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
287-335 1.27e-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: 1.27e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRI-KFGKLSLKCRDCRVVSHPECRDRCPLPC 335
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 ...
287-336 1.51e-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: 1.51e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPCI 336
Cdd:cd20843  12 HTFVIHSYTRPTVCQFCKKLLKgLFRQGLQCKDCKFNCHKRCATRVPNDCL 62
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
287-335 1.88e-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: 36.49  E-value: 1.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIkFG--KLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20793   1 HKFKVHTYYSPTFCDHCGSLL-YGlvRQGLKCKDCGMNVHHRCKENVPHLC 50
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
287-347 1.95e-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: 37.30  E-value: 1.95e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPCIPTLI--GTPVKIG 347
Cdd:cd20844   6 HTFAVHSYTRPTICQYCKRLLKgLFRQGMQCKDCRFNCHKRCASKVPRDCLGEVTfnGEPASPG 69
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
13-105 2.34e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361397     13 EQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVK---LKHARNQVDVEIKRRQR- 88
Cdd:TIGR02168  210 EKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQKe 289
                           90       100
                   ....*....|....*....|
gi 21361397     89 ---AEADCEKLERQIQLIRE 105
Cdd:TIGR02168  290 lyaLANEISRLEQQKQILRE 309
C1_ARHGEF2 cd20877
protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange ...
287-332 3.06e-03

protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange factor 2 (ARHGEF2) and similar proteins; ARHGEF2, also called guanine nucleotide exchange factor H1 (GEF-H1), microtubule-regulated Rho-GEF, or proliferating cell nucleolar antigen p40, acts as 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. ARHGEF2 may be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. It contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. 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: 410427  Cd Length: 61  Bit Score: 36.48  E-value: 3.06e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIKfGKLSLKCRDCRVVSHPECRDRCP 332
Cdd:cd20877   6 HLFTTITVSGTTMCSACNKSIT-AKEALICPTCNVTIHNRCKDTLP 50
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
287-335 4.06e-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: 35.73  E-value: 4.06e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20796   2 HTFVVHTYTKPTVCQHCKKLLKgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
287-335 6.21e-03

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


Pssm-ID: 410348  Cd Length: 54  Bit Score: 35.17  E-value: 6.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21361397 287 HDFVSKTVIKPESCVPCGKRIK-FGKLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20798   2 HTLAEHNYKKPTVCKVCDKLLVgLVRQGLKCRDCGVNVHKKCASLLPSNC 51
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
286-335 9.83e-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: 34.91  E-value: 9.83e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21361397 286 LHDFVSKTVIKPESCVPCGKRIkFG--KLSLKCRDCRVVSHPECRDRCPLPC 335
Cdd:cd20860   2 PHNFQETTYLKPTFCDNCAGFL-WGviKQGYRCKDCGMNCHKQCKDLVVFEC 52
 
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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