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Conserved domains on  [gi|568941565|ref|XP_006506043|]
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rho GTPase-activating protein 25 isoform X3 [Mus musculus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10138197)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 38-236 2.34e-140

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: 402.98  E-value: 2.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  38 AVFGQRLDETVAYEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASL 117
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 118 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 197
Cdd:cd04390   81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568941565 198 VIGVNLIRSKVEDPAVIMRGTPQIQRVMTMMIRDHEVLF 236
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 427-525 2.35e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   427 NSGEDDLDSLQRTVQSLQKEIETQKQV---YEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDV 503
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                           90       100
                   ....*....|....*....|..
gi 568941565   504 EKRNRVLEEEVKEFVKSMEKPK 525
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKR 916
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 38-236 2.34e-140

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: 402.98  E-value: 2.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  38 AVFGQRLDETVAYEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASL 117
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 118 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 197
Cdd:cd04390   81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568941565 198 VIGVNLIRSKVEDPAVIMRGTPQIQRVMTMMIRDHEVLF 236
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 59-232 4.03e-57

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 188.24  E-value: 4.03e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565    59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEG 137
Cdd:smart00324   3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDlSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   138 FLLCGQLMNADEAKaqQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIMrG 217
Cdd:smart00324  83 FIEAAKLEDETERL--RALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLK-D 159

                          170
                   ....*....|....*
gi 568941565   218 TPQIQRVMTMMIRDH 232
Cdd:smart00324 160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 60-208 3.61e-51

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.57  E-value: 3.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   60 PILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEGF 138
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDlEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  139 LLCGQLMNADEAKaqQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKV 208
Cdd:pfam00620  81 IEAAKLPDEEERL--EALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 427-525 2.35e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   427 NSGEDDLDSLQRTVQSLQKEIETQKQV---YEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDV 503
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                           90       100
                   ....*....|....*....|..
gi 568941565   504 EKRNRVLEEEVKEFVKSMEKPK 525
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKR 916
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 419-525 5.10e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.00  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  419 SEMEAGSKNSGEDDLDSLQRTVQSLQKEIETQKQVY----------EEQIKNLEKENYDVWAKVVRLNEELERERKKFAA 488
Cdd:pfam06160 324 NENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYselqeeleeiLEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568941565  489 LEISLRNVERSredVEKRN------------RVLEEEVKEFVKSMEKPK 525
Cdd:pfam06160 404 FKLELREIKRL---VEKSNlpglpesyldyfFDVSDEIEDLADELNEVP 449
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
430-527 6.17e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLQKEIETqkqvYEEQIKNLEKENYDVWAKVVRLNE---ELERERKKFAALEISLRNVERSREDVEKR 506
Cdd:PRK03918 199 EKELEEVLREINEISSELPE----LREELEKLEKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100
                 ....*....|....*....|.
gi 568941565 507 NRVLEEEVKEfVKSMEKPKTK 527
Cdd:PRK03918 275 IEELEEKVKE-LKELKEKAEE 294
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 437-524 1.41e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 437 QRTVQSLQKEIETQKqvyeEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSRE----DVEKRNRVLEE 512
Cdd:COG1579   88 NKEYEALQKEIESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEA 163

                         90
                 ....*....|..
gi 568941565 513 EVKEFVKSMEKP 524
Cdd:COG1579  164 EREELAAKIPPE 175
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 38-236 2.34e-140

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: 402.98  E-value: 2.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  38 AVFGQRLDETVAYEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASL 117
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 118 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 197
Cdd:cd04390   81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568941565 198 VIGVNLIRSKVEDPAVIMRGTPQIQRVMTMMIRDHEVLF 236
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 60-231 1.56e-57

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


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 189.05  E-value: 1.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  60 PILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQYEGFL 139
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 140 LCGQLMnaDEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIMRgTP 219
Cdd:cd00159   81 ELAKIE--DEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLED-IK 157

                        170
                 ....*....|..
gi 568941565 220 QIQRVMTMMIRD 231
Cdd:cd00159  158 KLNEIVEFLIEN 169
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 59-232 4.03e-57

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 188.24  E-value: 4.03e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565    59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEG 137
Cdd:smart00324   3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDlSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   138 FLLCGQLMNADEAKaqQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIMrG 217
Cdd:smart00324  83 FIEAAKLEDETERL--RALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLK-D 159

                          170
                   ....*....|....*
gi 568941565   218 TPQIQRVMTMMIRDH 232
Cdd:smart00324 160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 60-208 3.61e-51

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.57  E-value: 3.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   60 PILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEGF 138
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDlEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  139 LLCGQLMNADEAKaqQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKV 208
Cdd:pfam00620  81 IEAAKLPDEEERL--EALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 37-237 2.20e-34

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: 128.73  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  37 KAVFGQRLDEtvayeqkfgpHL------VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAG--ERPSFDRD 108
Cdd:cd04386    2 KPVFGTPLEE----------HLkrtgreIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtfSLPLDEFY 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 109 TDVHTVASLLKLYLRDLPEPVVPWSQYEGFLlcgQLMN-ADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAV 187
Cdd:cd04386   72 SDPHAVASALKSYLRELPDPLLTYNLYEDWV---QAANkPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDE 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568941565 188 NKMSVDNLATVIGVNLIRSKVEDPAVIMRGTPQIQRVMT--MMIRDHEVLFP 237
Cdd:cd04386  149 NKMSPSNIAIVLAPNLLWAKNEGSLAEMAAGTSVHVVAIveLIISHADWFFP 200
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 39-210 4.71e-34

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: 127.19  E-value: 4.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  39 VFGQRLDETvayeQKFG--PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVAS 116
Cdd:cd04393    2 VFGVPLQEL----QQAGqpENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAAS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 117 LLKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQeLVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLA 196
Cdd:cd04393   78 LLRLFLQELPEGLIPASLQIRLMQLYQDYNGEDEFGRK-LRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLA 156

                        170
                 ....*....|....*.
gi 568941565 197 TVIGVNL--IRSKVED 210
Cdd:cd04393  157 AVFGPDVfhVYTDVED 172
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 59-241 1.14e-32

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: 124.09  E-value: 1.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQYEGF 138
Cdd:cd04376    9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 139 LLCGQLMNADEAKAQQELVKQLSTLPRDN-YNLLSyicrFLHEIQLNCAV-----------NKMSVDNLATVIGVNLIR- 205
Cdd:cd04376   89 IGTALLEPDEQLEALQLLIYLLPPCNCDTlHRLLK----FLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLHk 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568941565 206 -----SKVEDPAVIMRGTPQIQRVMTMMIRDHEVLFPKSKD 241
Cdd:cd04376  165 qksgeREFVQASLRIEESTAIINVVQTMIDNYEELFMVSPE 205
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 55-236 2.86e-30

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: 117.05  E-value: 2.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  55 GPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQ 134
Cdd:cd04404   19 EQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEDVHLPAVILKTFLRELPEPLLTFDL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 135 YEGFLLCGQLMNADEAKAQQELVKqlsTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKveDPAVI 214
Cdd:cd04404   99 YDDIVGFLNVDKEERVERVKQLLQ---TLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPNLLWAK--DASMS 173

                        170       180
                 ....*....|....*....|..
gi 568941565 215 MRGTPQIQRVMTMMIRDHEVLF 236
Cdd:cd04404  174 LSAINPINTFTKFLLDHQDEIF 195
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 40-204 1.42e-29

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: 114.81  E-value: 1.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  40 FGQRLDETVAYEQKfgphLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGER-----PSFDRDTDVHTV 114
Cdd:cd04398    1 FGVPLEDLILREGD----NVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLnvlliSPEDYESDIHSV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 115 ASLLKLYLRDLPEPVVPWSQYEGFLLCGqlMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDN 194
Cdd:cd04398   77 ASLLKLFFRELPEPLLTKALSREFIEAA--KIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNN 154

                        170
                 ....*....|
gi 568941565 195 LATVIGVNLI 204
Cdd:cd04398  155 LAIIWGPTLM 164
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 39-198 4.63e-29

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 113.61  E-value: 4.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  39 VFGQRLDETVAYE-QKFGPHLVPILVEKCAEFILEHG-VSEEGIFRLPGQDNLVKQLRDAFDAGerpsFDRDT------- 109
Cdd:cd04400    1 IFGSPLEEAVELSsHKYNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTE----YDVDLfssslyp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 110 DVHTVASLLKLYLRDLPEPVVPWSQYEGFLLCGQLmNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNK 189
Cdd:cd04400   77 DVHTVAGLLKLYLRELPTLILGGELHNDFKRLVEE-NHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNK 155


                 ....*....
gi 568941565 190 MSVDNLATV 198
Cdd:cd04400  156 MNLRNVCIV 164
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 39-206 6.02e-28

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: 110.57  E-value: 6.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  39 VFGQRLDET-VAYEQKFgphlVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAG--ERPSFD-RDTDVHTV 114
Cdd:cd04395    1 TFGVPLDDCpPSSENPY----VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGgfDIDLQDpRWRDVNVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 115 ASLLKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAkaQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDN 194
Cdd:cd04395   77 SSLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVER--LKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRN 154

                        170
                 ....*....|..
gi 568941565 195 LATVIGVNLIRS 206
Cdd:cd04395  155 LAIVFGPTLVRT 166
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 40-229 3.72e-27

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: 107.86  E-value: 3.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  40 FGQRLDETVAYEQKFGPHL-VPILVEKCAEFILEHGVSE-EGIFRLPGQDNLVKQLRDAFDAGERPSFDRDtDVHTVASL 117
Cdd:cd04389    1 FGSSLEEIMDRQKEKYPELkLPWILTFLSEKVLALGGFQtEGIFRVPGDIDEVNELKLRVDQWDYPLSGLE-DPHVPASL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 118 LKLYLRDLPEPVVPWSQYEGfllCgqLMNADEAKAQQELVKqlsTLPRDNYNLLSYICRFLHE--IQLNCAVNKMSVDNL 195
Cdd:cd04389   80 LKLWLRELEEPLIPDALYQQ---C--ISASEDPDKAVEIVQ---KLPIINRLVLCYLINFLQVfaQPENVAHTKMDVSNL 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568941565 196 ATVIGVNLIRSKVEDPAVIMRGTPQIQRVMTMMI 229
Cdd:cd04389  152 AMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLI 185
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 56-236 4.56e-27

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: 107.99  E-value: 4.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  56 PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDA-GERPSFDRDT--DVHTVASLLKLYLRDLPEPVVPW 132
Cdd:cd04372   13 NTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdGEKADISATVypDINVITGALKLYFRDLPIPVITY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 133 SQYEGFLLCGQLMNADEakaQQELVKQ-LSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDP 211
Cdd:cd04372   93 DTYPKFIDAAKISNPDE---RLEAVHEaLMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSA 169

                        170       180
                 ....*....|....*....|....*.
gi 568941565 212 AVIMRG-TPQIQrVMTMMIRDHEVLF 236
Cdd:cd04372  170 LTTLNDmRYQIL-IVQLLITNEDVLF 194
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 56-228 9.39e-27

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: 106.99  E-value: 9.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  56 PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQY 135
Cdd:cd04382   14 SPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 136 EGFLLCGQlmNADEAKAQQELVKQLSTLPRDNYNLLSYIcrFLHeIQ--LNCAVNKMSVDNLATVIGVNLIRSKVEDP-- 211
Cdd:cd04382   94 KEFMEAAE--ILDEDNSRAALYQAISELPQPNRDTLAFL--ILH-LQrvAQSPECKMDINNLARVFGPTIVGYSVPNPdp 168

                        170
                 ....*....|....*..
gi 568941565 212 AVIMRGTPQIQRVMTMM 228
Cdd:cd04382  169 MTILQDTVRQPRVVERL 185
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 59-207 5.40e-26

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 104.89  E-value: 5.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  59 VPILVEKCAEFILEHGVSEeGIFRLPGQDNLVKQLRDAFDAGERPSFDRDT---DVHTVASLLKLYLRDLPEPVVPWSQY 135
Cdd:cd04384   18 VPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQIPDLTKDVyiqDIHSVSSLCKLYFRELPNPLLTYQLY 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941565 136 EGFLlcgQLMNADEAKAQQELVKQ-LSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSK 207
Cdd:cd04384   97 EKFS---EAVSAASDEERLEKIHDvIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAPNLLRSK 166
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 59-203 1.74e-24

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: 100.46  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERP-SFDRDTD-VHTVASLLKLYLRDLPEPVVPWSQYE 136
Cdd:cd04385   15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSvQLREGEYtVHDVADVLKRFLRDLPDPLLTSELHA 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941565 137 GFLLCGQLMNADEA-KAQQELvkqLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNL 203
Cdd:cd04385   95 EWIEAAELENKDERiARYKEL---IRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTL 159
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 40-231 2.01e-24

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: 100.21  E-value: 2.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  40 FGQRLDETVAYEqkfgpHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLK 119
Cdd:cd04377    1 FGVSLSSLTSED-----RSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 120 LYLRDLPEPVVPWSQYEGFLlcgqlmNADEAKAQQELVKQLST----LPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNL 195
Cdd:cd04377   76 QWLRELPEPLMTFELYENFL------RAMELEEKQERVRALYSvleqLPRANLNTLERLIFHLVRVALQEEVNRMSANAL 149

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568941565 196 ATVIGVNLIRS-KVEDPAVIMRGTPQIQRVMTMMIRD 231
Cdd:cd04377  150 AIVFAPCILRCpDTADPLQSLQDVSKTTTCVETLIKE 186
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 40-205 1.63e-23

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 97.88  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  40 FGQRLDETVayeqKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD--RDTDVHTVASL 117
Cdd:cd04383    3 FNGSLEEYI----QDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADdqNDHDINSVAGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 118 LKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELVkqLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLAT 197
Cdd:cd04383   79 LKLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREI--LSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAI 156


                 ....*...
gi 568941565 198 VIGVNLIR 205
Cdd:cd04383  157 CFGPTLMP 164
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 58-210 2.40e-23

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: 97.69  E-value: 2.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  58 LVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERP--SFDRDTDVHTVASLLKLYLRDLPEPVVPWSQY 135
Cdd:cd04387   15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDvsVMLSEMDVNAIAGTLKLYFRELPEPLFTDELY 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941565 136 EGFLlcGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVED 210
Cdd:cd04387   95 PNFA--EGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKE 167
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 57-206 2.79e-23

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: 97.54  E-value: 2.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  57 HLVPILVEKCaEFILEHgVSEEGIFRLPGQDNLVKQLRDAFDAGErpsfDRDTDVHT--VASLLKLYLRDLPEPVVPWSQ 134
Cdd:cd04394   19 NVPKFLVDAC-TFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGE----ACLSSALPcdVAGLLKQFFRELPEPLLPYDL 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568941565 135 YEGFLLCGQLMNADEAKAQQELVKQLstLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRS 206
Cdd:cd04394   93 HEALLKAQELPTDEERKSATLLLTCL--LPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPNLFQS 162
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 54-225 1.80e-22

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: 94.77  E-value: 1.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  54 FGPHL----------VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD--RDTDVHTVASLLKLY 121
Cdd:cd04403    1 FGCHLealcqrenstVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDdsKWEDIHVITGALKLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 122 LRDLPEPVVPWSQYEGFLLCGQLMNA-DEAKAQQELVKQlstLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIG 200
Cdd:cd04403   81 FRELPEPLFPYSLFNDFVAAIKLSDYeQRVSAVKDLIKS---LPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFG 157

                        170       180
                 ....*....|....*....|....*..
gi 568941565 201 VNLIRSKVE--DPAVIMRGTPQIQRVM 225
Cdd:cd04403  158 PTLLRPEQEtgNIAVHMVYQNQIVELI 184
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 59-231 6.67e-22

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: 93.13  E-value: 6.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQYEGF 138
Cdd:cd04407   15 VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 139 LLCGQLMNADEakAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIR-SKVEDPAVIMRG 217
Cdd:cd04407   95 LRAVELPEKQE--QLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRcPDSSDPLTSMKD 172

                        170
                 ....*....|....
gi 568941565 218 TPQIQRVMTMMIRD 231
Cdd:cd04407  173 VAKTTTCVEMLIKE 186
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 39-198 1.41e-21

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


Pssm-ID: 239861  Cd Length: 225  Bit Score: 93.24  E-value: 1.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  39 VFGQRLDETVAYEQ-------------KFGphLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGER--P 103
Cdd:cd04396    1 VFGVSLEESLKYASvaisivdedgeqyVYG--YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDygK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 104 SFDRDT-DVHTVASLLKLYLRDLPEPVVPWSQYEGF---------------LLCGQLMNADEAKAQQELVKQLSTLPRDN 167
Cdd:cd04396   79 SFDWDGyTVHDAASVLRRYLNNLPEPLVPLDLYEEFrnplrkrprilqymkGRINEPLNTDIDQAIKEYRDLITRLPNLN 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568941565 168 YNLLSYICRFLHEIQLNCAVNKMSVDNLATV 198
Cdd:cd04396  159 RQLLLYLLDLLAVFARNSDKNLMTASNLAAI 189
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 40-199 3.34e-21

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: 90.96  E-value: 3.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  40 FGQRLDETVAYEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDrDTDVHTVASLLK 119
Cdd:cd04381    1 FGASLSLAVERSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLE-EYEPPTVASLLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 120 LYLRDLPEPVVP---WSQYEGflLCGQLmnaDEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLA 196
Cdd:cd04381   80 QYLRELPEPLLTkelMPRFEE--ACGRP---TEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNIS 154


                 ...
gi 568941565 197 TVI 199
Cdd:cd04381  155 IVL 157
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 56-215 1.72e-20

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: 89.79  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  56 PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQY 135
Cdd:cd04378   13 PDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 136 EGFL-LCGQLMNADEAKAQQEL----------VKQL-STLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNL 203
Cdd:cd04378   93 NDFIaLAKEIQRDTEEDKAPNTpievnriirkLKDLlRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTL 172

                        170
                 ....*....|..
gi 568941565 204 IRSKVEDPAVIM 215
Cdd:cd04378  173 IRPRPGDADVSL 184
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 59-205 1.23e-19

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: 86.74  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFD-RDTDVHTVASLLKLYLRDLPEPVVPWSQYEG 137
Cdd:cd04373   15 IPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVsKDFTVNAVAGALKSFFSELPDPLIPYSMHLE 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941565 138 flLCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIR 205
Cdd:cd04373   95 --LVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 57-236 2.19e-19

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: 86.20  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  57 HLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTdVHTVASLLKLYLRDLPEPVVPWSQYE 136
Cdd:cd04402   13 DNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDLKAEP-VLLLASVLKDFLRNIPGSLLSSDLYE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 137 GFLlcGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVeDPAVIMR 216
Cdd:cd04402   92 EWM--SALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPPA-SSELQNE 168

                        170       180
                 ....*....|....*....|
gi 568941565 217 GTPQIQRVMTMMIRDHEVLF 236
Cdd:cd04402  169 DLKKVTSLVQFLIENCQEIF 188
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 39-236 5.07e-18

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


Pssm-ID: 239856  Cd Length: 216  Bit Score: 82.78  E-value: 5.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  39 VFGQRLDETVAYEQKFGPHL-VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAgerPSFDRDTD-----VH 112
Cdd:cd04391    1 LFGVPLSTLLERDQKKVPGSkVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEA---KFYEGTFLwdqvkQH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 113 TVASLLKLYLRDLPEPVVPWSQYEGFLLCGQLMN-ADEAKAQQELVKqlsTLPRDNYNLLSYICRFLHEIQLNCAVNKMS 191
Cdd:cd04391   78 DAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSkKDQLQALNLLVL---LLPEANRDTLKALLEFLQKVVDHEEKNKMN 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568941565 192 VDNLATVIGVNL-----IRSK-VEDPAVIMRGTPQIQRVMTMMIRDHEVLF 236
Cdd:cd04391  155 LWNVAMIMAPNLfpprgKHSKdNESLQEEVNMAAGCANIMRLLIRYQDLLW 205
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 40-213 6.51e-18

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: 82.55  E-value: 6.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  40 FGQRLDETVayeqKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLK 119
Cdd:cd04409    1 FGADFAQVA----KKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 120 LYLRDLPEPVVPWSQYEGFL-LCGQLMNADEAKAQQELV--KQLST-----------------LPRDNYNLLSYICRFLH 179
Cdd:cd04409   77 LYLRQLPEPLILFRLYNEFIgLAKESQHVNETQEAKKNSdkKWPNMctelnrillkskdllrqLPAPNYNTLQFLIVHLH 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568941565 180 EIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAV 213
Cdd:cd04409  157 RVSEQAEENKMSASNLGIIFGPTLIRPRPTDATV 190
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 63-215 1.38e-17

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: 81.29  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  63 VEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAF------DAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQYE 136
Cdd:cd04374   32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktsTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 137 GFLLCGQLMNAD-EAKAQQELVKQlstLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIM 215
Cdd:cd04374  112 DFINAAKSENLEsRVNAIHSLVHK---LPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAIM 188
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 56-205 2.52e-17

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: 80.25  E-value: 2.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  56 PHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQY 135
Cdd:cd04408   13 PEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPFQLY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 136 EGFLLCGQLMNADEAKAQ----------QELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIR 205
Cdd:cd04408   93 DDFIALAKELQRDSEKAAespsiveniiRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLR 172
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 71-236 2.77e-17

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: 80.58  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  71 LEHGVSEEGIFRLPGqdNLVKQ--LRDAFDAGERPSFDR-DTDVHTVASLLKLYLRDLPEPVVPWSQYEGFLLCGQLMNA 147
Cdd:cd04392   20 LEKNLRVEGLFRKPG--NSARQqeLRDLLNSGTDLDLESgGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLCQF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 148 DE------AKAQQELVKQLS----TLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIMRG 217
Cdd:cd04392   98 DEkgnktsAPDKERLLEALQllllLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHEN 177

                        170
                 ....*....|....*....
gi 568941565 218 TPQIQRVMTMMIRDHEVLF 236
Cdd:cd04392  178 AQKLNSIVTFMIKHSQKLF 196
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 59-205 1.28e-16

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: 78.12  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAGERPSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQYEGF 138
Cdd:cd04406   15 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEF 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941565 139 LLCGQLMNADEA-KAQQELVKQLStlpRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIR 205
Cdd:cd04406   95 LRAMGLQERRETvRGVYSVIDQLS---RTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILR 159
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 65-231 3.28e-16

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: 77.77  E-value: 3.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  65 KCAEFILEHGVSEEGIFRLPGQDN----LVKQLRDAFDAGErpSFDRDTDVHTVASLLKLYLRDLPEPVVPWSQYEGFLL 140
Cdd:cd04380   56 RLVDYLYTRGLAQEGLFEEPGLPSepgeLLAEIRDALDTGS--PFNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 141 CGQlmNADEAKAQqeLVKqlSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVIMRGTPQ 220
Cdd:cd04380  134 AVA--NNEEDKRQ--VIR--ISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAERD 207

                        170
                 ....*....|...
gi 568941565 221 --IQRVMTMMIRD 231
Cdd:cd04380  208 rkRAFIEQFLLND 220
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 40-210 3.98e-16

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: 77.12  E-value: 3.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  40 FGQRLDETVayEQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFD---AGERPSFDRDTDVHTVAS 116
Cdd:cd04379    1 FGVPLSRLV--EREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFErnsAAVELSEELYPDINVITG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 117 LLKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEAKAQQELV-KQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNL 195
Cdd:cd04379   79 VLKDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTlSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNL 158

                        170
                 ....*....|....*
gi 568941565 196 ATVIGVNLIRSKVED 210
Cdd:cd04379  159 AVCFGPVLMFCSQEF 173
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 59-211 1.37e-14

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: 72.78  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  59 VPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDAG--ERPSFDRDTDVHtVASLLKLYLRDLPEPVVPWSQYE 136
Cdd:cd04397   27 IPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNptEVPDLSKENPVQ-LAALLKKFLRELPDPLLTFKLYR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 137 GFLLCGQLmnADEAKAQQELVKQLSTLPRDNYNLLSYICRFL------HEIQlNCAVNKMSVDNLATVIGVNLIRSKVED 210
Cdd:cd04397  106 LWISSQKI--EDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLkwvssfSHID-EETGSKMDIHNLATVITPNILYSKTDN 182


                 .
gi 568941565 211 P 211
Cdd:cd04397  183 P 183
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 37-241 4.23e-12

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: 65.52  E-value: 4.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  37 KAVFGQRLDETVayeQKFGpHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVKQLRDAFDA-GERPSFDrDTDVHTVA 115
Cdd:cd04375    2 KNVFGVPLLVNL---QRTG-QPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESsTDNVNYD-GQQAYDVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 116 SLLKLYLRDLPEPVVPWSQYEGFLLCGQLMNADEakaQQELVK-QLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDN 194
Cdd:cd04375   77 DMLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQ---RLEAVQcAILLLPDENREVLQTLLYFLSDVAANSQENQMTATN 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941565 195 LA-----TVIGVNLIRSKVEDPAVIMR-----GTPQ---------IQRVMTMMIRDHEVLFPKSKD 241
Cdd:cd04375  154 LAvclapSLFHLNTSRRENSSPARRMQrkkslGKPDqkelsenkaAHQCLAYMIEECNTLFMVPKE 219
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 88-214 5.00e-06

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


Pssm-ID: 239864  Cd Length: 212  Bit Score: 47.71  E-value: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  88 NLVKQLRDAFDAGERPSFDR----DTDVHTVASLLKLYLRDLPEPVVPWSQYEgfLLCGQLMN------ADEAKAQQELV 157
Cdd:cd04399   51 KETHQLRNLLNKPKKPDKEViilkKFEPSTVASVLKLYLLELPDSLIPHDIYD--LIRSLYSAyppsqeDSDTARIQGLQ 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 158 KQLSTLPRDNYNLLSYICRFLH---EIQLNCAVNKMSVDNLATVIGVNLIRSKVEDPAVI 214
Cdd:cd04399  129 STLSQLPKSHIATLDAIITHFYrliEITKMGESEEEYADKLATSLSREILRPIIESLLTI 188
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 51-208 7.11e-06

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 46.79  E-value: 7.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  51 EQKFGPHLVPILVEKCAEFILEHGVSEEGIFRLPGQDNLVkQLRDAFDAgERPSFDRDT-DVHTVASLLKLYLRDLPEPV 129
Cdd:cd04388    7 EQFSPPDVAPPLLIKLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDC-DAASVDLEQfDVAALADALKRYLLDLPNPV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 130 VPWSQYEGFL-LCGQLMNADEAKAQQELVKQLSTLPRDNYNLLSYICRFLHEIQLNCAVNKMSVDNLATVIGVNLIRSKV 208
Cdd:cd04388   85 IPAPVYSEMIsRAQEVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQP 164
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 427-525 2.35e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   427 NSGEDDLDSLQRTVQSLQKEIETQKQV---YEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDV 503
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                           90       100
                   ....*....|....*....|..
gi 568941565   504 EKRNRVLEEEVKEFVKSMEKPK 525
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKR 916
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 419-525 5.10e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.00  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  419 SEMEAGSKNSGEDDLDSLQRTVQSLQKEIETQKQVY----------EEQIKNLEKENYDVWAKVVRLNEELERERKKFAA 488
Cdd:pfam06160 324 NENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYselqeeleeiLEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568941565  489 LEISLRNVERSredVEKRN------------RVLEEEVKEFVKSMEKPK 525
Cdd:pfam06160 404 FKLELREIKRL---VEKSNlpglpesyldyfFDVSDEIEDLADELNEVP 449
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
430-527 6.17e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLQKEIETqkqvYEEQIKNLEKENYDVWAKVVRLNE---ELERERKKFAALEISLRNVERSREDVEKR 506
Cdd:PRK03918 199 EKELEEVLREINEISSELPE----LREELEKLEKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100
                 ....*....|....*....|.
gi 568941565 507 NRVLEEEVKEfVKSMEKPKTK 527
Cdd:PRK03918 275 IEELEEKVKE-LKELKEKAEE 294
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 426-526 7.35e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 7.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  426 KNSGEDDLDSLQRTVQSLQKEIETQKQV---YEEQIKN-------LEKENYDVWAKVVRLNEELERERKKFAALEISLRN 495
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLnqqKDEQIKKlqqekelLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568941565  496 VERSREDVEKRNRVLEEEVKEFVKSMEKPKT 526
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 437-524 1.41e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 437 QRTVQSLQKEIETQKqvyeEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSRE----DVEKRNRVLEE 512
Cdd:COG1579   88 NKEYEALQKEIESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEA 163

                         90
                 ....*....|..
gi 568941565 513 EVKEFVKSMEKP 524
Cdd:COG1579  164 EREELAAKIPPE 175
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 430-529 1.94e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  430 EDDLDSLQRTVQSLQKEIETQKQ---VYEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDVEK- 505
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKEtiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKe 490

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568941565  506 -------------RNRVLEEEVKEFVKSMEKPKTKTD 529
Cdd:TIGR04523 491 lkskekelkklneEKKELEEKVKDLTKKISSLKEKIE 527
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 431-523 4.44e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 431 DDLDSLQRTVQSLQKEIETQKQVYEE---QIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDVEKRN 507
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90
                 ....*....|....*.
gi 568941565 508 RVLEEEVKEFVKSMEK 523
Cdd:COG4942  100 EAQKEELAELLRALYR 115
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 406-519 5.94e-04

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: 42.74  E-value: 5.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   406 ASDSKRDALVSTDSEMEagsknsgeDDLDSLQRTVQSLQKEI---ETQKQVYEEQIKNLEKENYDVWA------------ 470
Cdd:TIGR02168  264 ELEEKLEELRLEVSELE--------EEIEELQKELYALANEIsrlEQQKQILRERLANLERQLEELEAqleeleskldel 335

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568941565   471 --KVVRLNEELERERKKFAALEISLRNVERSREDVEKRNRVLEEEVKEFVK 519
Cdd:TIGR02168  336 aeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 413-530 8.79e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   413 ALVSTDSEMEAGSKNSGEDDLDSLQRTVQSLQKEIET----------QKQVYEEQIKNLEKENYDVWAKVVRLNEELERE 482
Cdd:TIGR02169  269 EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlersiaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941565   483 RKKFAALEISL------RNVERSR-EDVEKRNRVLEEEVKEFVKSMEKPKTKTDP 530
Cdd:TIGR02169  349 RKRRDKLTEEYaelkeeLEDLRAElEEVDKEFAETRDELKDYREKLEKLKREINE 403
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
410-523 9.27e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 9.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 410 KRDALVSTDSEmeagSKNSGEDDLDSLQRTVQSLQKEIE---TQKQVYEEQIKNLEKENYDVWAKVVRLNEELERERKKF 486
Cdd:COG4372   21 KTGILIAALSE----QLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568941565 487 AALEISLRNVERSREDVEKRNRVLEEEVKEFVKSMEK 523
Cdd:COG4372   97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 387-518 9.50e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 40.30  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  387 NVPTSPQSQGNPAGALSPPASDSKRDALVSTDSEMEAGSKNSGE--DDLDSLQRTVQSLQKEIETQkqvyEEQIKNLEKE 464
Cdd:pfam08614  32 SVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGElaQRLVDLNEELQELEKKLRED----ERRLAALEAE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941565  465 NYDVWAKVVRLNEELERERKKFAAL--EISLRNVERSRedVEKRNRVLEEEVKEFV 518
Cdd:pfam08614 108 RAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM--AEEKLRKLEKENRELV 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 423-523 1.56e-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: 41.58  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   423 AGSKNSGEDDLDSLQRTVQSLQKEIETQKQVYEEQIKNLEKENydvwAKVVRLNEELERERKKFAALEISLRNVERSRED 502
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNEEAANLRERLESLERRIAA 835

                           90       100
                   ....*....|....*....|.
gi 568941565   503 VEKRNRVLEEEVKEFVKSMEK 523
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIES 856
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 411-516 1.59e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 411 RDALVSTDSEMEAGSKNSGEDDLDSLQRTVQSLQKEIETQKQVYEEQIKNLEKENydvwAKVVRLNEELERERKKFAALE 490
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ----AEEYELLAELARLEQDIARLE 308

                         90       100
                 ....*....|....*....|....*.
gi 568941565 491 ISLRNVERSREDVEKRNRVLEEEVKE 516
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEE 334
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
430-514 1.97e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLQKEIETQKQ----VYEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDVEK 505
Cdd:COG4717  162 EEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241


                 ....*....
gi 568941565 506 RNRVLEEEV 514
Cdd:COG4717  242 EERLKEARL 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 430-527 2.24e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   430 EDDLDSLQRTVQSLQKEIETQkqvyEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDVEKRNRV 509
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEEL----SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                           90
                   ....*....|....*...
gi 568941565   510 LEEEVKEFVKSMEKPKTK 527
Cdd:TIGR02168  906 LESKRSELRRELEELREK 923
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 398-530 2.43e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   398 PAGALSPPASDSKRDALVSTDSEMEAGSKNsgeDDLDSLQRTVQSLQKEIETQKQ----------VYEEQIKNLEKENYD 467
Cdd:TIGR02169  651 KSGAMTGGSRAPRGGILFSRSEPAELQRLR---ERLEGLKRELSSLQSELRRIENrldelsqelsDASRKIGEIEKEIEQ 727

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941565   468 VWAKVVRLNEELERERKKFAALEISLRNVERSREDVEKRNRVLEEEVKEFVKSMEKPKTKTDP 530
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
408-527 2.54e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 408 DSKRDALVSTDSEMEAGSKNSGE-----DDLDSLQRTVQSLQKE---IETQKQVYEEQIKNLEKENYDVWAKVVRLnEEL 479
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKEleelkEEIEELEKELESLEGSkrkLEEKIRELEERIEELKKEIEELEEKVKEL-KEL 288

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568941565 480 ERERKKFAALEISLRNVERSREDVEKRNRVLEEEVKEFVKSMEKPKTK 527
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 439-516 3.72e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 38.89  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  439 TVQSLQKEIETQKQVYEEQIKNLEKEN--YDVW-----AKVVRLNEELERERKK----FAALEISLRNVERSREDVEKRn 507
Cdd:pfam05010 104 VISGYKKNEESLKKCAQDYLARIKKEEqrYQALkahaeEKLDQANEEIAQVRSKakaeTAALQASLRKEQMKVQSLERQ- 182


                  ....*....
gi 568941565  508 rvLEEEVKE 516
Cdd:pfam05010 183 --LEQKTKE 189
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
430-523 4.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLQKEIETQKQVYEEQIKNLE--KENYDVwAKVVRLNEELERERKKFAALEISLRNVERSREDVEKRN 507
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEelEKKYSE-EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696

                         90
                 ....*....|....*.
gi 568941565 508 RVLEEEVKEFVKSMEK 523
Cdd:PRK03918 697 EKLKEELEEREKAKKE 712
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
430-529 4.67e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLQKEI---ETQKQVYEEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERsredvEKR 506
Cdd:COG4372  107 QEEAEELQEELEELQKERqdlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE-----AEA 181

                         90       100
                 ....*....|....*....|...
gi 568941565 507 NRVLEEEVKEFVKSMEKPKTKTD 529
Cdd:COG4372  182 EQALDELLKEANRNAEKEEELAE 204
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
408-516 4.80e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 408 DSKRDALVSTDSEMEAGSK--NSGEDDLDSLQRTVQSLQKEIETQKQVY---EEQIKNLEKENYDVWAKVVRLNEELERE 482
Cdd:COG4372   48 EQLREELEQAREELEQLEEelEQARSELEQLEEELEELNEQLQAAQAELaqaQEELESLQEEAEELQEELEELQKERQDL 127

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568941565 483 RKKFAALEISLRNVERSREDVEKRNRVLEEEVKE 516
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 446-523 5.86e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.82  E-value: 5.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941565  446 EIETQKQVYEEQIKNLEKENYdvwakvvRLNEELERERKKFAALEISLRNVERSREDVEKRNRVLEEEVKEFVKSMEK 523
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETK-------KAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEM 73
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
430-512 5.99e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLQKEIETQKQVYEE---QIKNLEK--ENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDVE 504
Cdd:COG4717   87 EEEYAELQEELEELEEELEELEAELEElreELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166


                 ....*...
gi 568941565 505 KRNRVLEE 512
Cdd:COG4717  167 ELEAELAE 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 445-523 7.67e-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: 39.27  E-value: 7.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   445 KEIETQKQVYEEQIKNLEKE-------NYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDVEKRNRVLEEEVKEF 517
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKAlaelrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759


                   ....*.
gi 568941565   518 VKSMEK 523
Cdd:TIGR02168  760 EAEIEE 765
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 412-529 8.42e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 8.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565   412 DALVSTDSEMEAGSKNSGEddldslqrtVQSLQKEIETQKQVYEEQIKNLEKENYdvwAKVVRLNEELERER-------- 483
Cdd:pfam01576  310 DTLDTTAAQQELRSKREQE---------VTELKKALEEETRSHEAQLQEMRQKHT---QALEELTEQLEQAKrnkanlek 377

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568941565   484 ------KKFAALEISLRNVERSREDVEKRNRVLEEEVKEF-VKSMEKPKTKTD 529
Cdd:pfam01576  378 akqaleSENAELQAELRTLQQAKQDSEHKRKKLEGQLQELqARLSESERQRAE 430
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
430-527 9.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 9.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLqKEIETQKQVYEEQIKNLEKENYDVWAKVVRLN----EELE---RERKKFAALEISLRNVERSRED 502
Cdd:PRK03918 538 KGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEerlKELEPFYNEYLELKDAEKELER 616

                         90       100
                 ....*....|....*....|....*
gi 568941565 503 VEKRNRVLEEEVKEFVKSMEKPKTK 527
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKR 641
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 435-529 9.22e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565  435 SLQRTVQSLQKEIETQKQVY---EEQIKNLEKENYDVWAKVVRLNEELERERKKFAALEISLRNVERSREDVEK-RNRVL 510
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEIsntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqKEQDW 308

                          90
                  ....*....|....*....
gi 568941565  511 EEEVKEFVKSMEKPKTKTD 529
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQ 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 430-516 9.33e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 9.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941565 430 EDDLDSLQRTVQSLQKEIETQKQVYEEQIKNLEKENYDVWAKVVRLNEELERerkkFAAL------EISLRNVE-RSRED 502
Cdd:PRK12704  95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER----ISGLtaeeakEILLEKVEeEARHE 170

                         90
                 ....*....|....
gi 568941565 503 VEKRNRVLEEEVKE 516
Cdd:PRK12704 171 AAVLIKEIEEEAKE 184
 
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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