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Conserved domains on  [gi|1720365289|ref|XP_030101672|]
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rho GTPase-activating protein 44 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
1-167 1.78e-112

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


The actual alignment was detected with superfamily member cd07619:

Pssm-ID: 472257  Cd Length: 248  Bit Score: 340.10  E-value: 1.78e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAG 80
Cdd:cd07619    82 MLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPTG 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  81 AKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSF 160
Cdd:cd07619   162 AKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPSY 241

                  ....*..
gi 1720365289 161 GKPLEEH 167
Cdd:cd07619   242 GKPLEEH 248
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
156-356 7.99e-102

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.


The actual alignment was detected with superfamily member cd04386:

Pssm-ID: 470621  Cd Length: 203  Bit Score: 310.54  E-value: 7.99e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 156 EKPSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 233
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 234 LKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVL 313
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720365289 314 GPNLLWPQSEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEI 356
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
PHA03247 super family cl33720
large tegument protein UL36; Provisional
436-716 7.70e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 7.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  436 GSSAGRKASCAPPSMQPPAPPSELAAPLPSPLPEQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPG 515
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  516 SIQGTPCPGTQLGP------QPAASPSQLPADQSPHTLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQPSPVslsptppst 589
Cdd:PHA03247  2868 SRSPAAKPAAPARPpvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR--------- 2938
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  590 pspyglsyPPGYSMASGQLSPASAPPLASPSVFTSTLAKSRpTPKPRQRptlPPPQPPSVSLSASSPQSTEHPMLDGMSp 669
Cdd:PHA03247  2939 --------PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR-VAVPRFR---VPQPAPSREAPASSTPPLTGHSLSRVS- 3005
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720365289  670 geSMSTDL-VHFDVPSIHIELGSTLRLSP-LEHARRHSA--TDKRDSEEES 716
Cdd:PHA03247  3006 --SWASSLaLHEETDPPPVSLKQTLWPPDdTEDSDADSLfdSDSERSDLEA 3054
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
1-167 1.78e-112

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 2 (Rich2) is a Rho GTPase activating protein that interacts with CD317, a lipid raft-associated integral membrane protein. It plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. Rich2 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153303  Cd Length: 248  Bit Score: 340.10  E-value: 1.78e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAG 80
Cdd:cd07619    82 MLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPTG 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  81 AKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSF 160
Cdd:cd07619   162 AKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPSY 241

                  ....*..
gi 1720365289 161 GKPLEEH 167
Cdd:cd07619   242 GKPLEEH 248
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
156-356 7.99e-102

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: 310.54  E-value: 7.99e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 156 EKPSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 233
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 234 LKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVL 313
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720365289 314 GPNLLWPQSEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEI 356
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
173-348 1.76e-59

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: 198.26  E-value: 1.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  173 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELY 251
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSeYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  252 DEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSEGNITEMMT 331
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 1720365289  332 TvslQIVGIIEPIIQHA 348
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
177-322 2.00e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 183.52  E-value: 2.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 177 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-VVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWI 255
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720365289 256 QASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQS 322
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-149 1.90e-35

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 134.00  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAeVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPag 80
Cdd:pfam03114  93 ALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKSSKAKDES-- 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  81 akadALREEMEEAANRVEICRDQLSADMYSFVAKEIDY-ANYFQTLIEVQAEYHRKSLTLLQAVLPQIKA 149
Cdd:pfam03114 170 ----QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
BAR smart00721
BAR domain;
1-149 5.32e-35

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 132.89  E-value: 5.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289    1 MLKLCGETEDKLAQELIHFeLQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTskssgLSSSLQPAG 80
Cdd:smart00721  96 ALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA-----KKSKEKKKD 169
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   81 AKADALREEMEEAANRVEICRDQLSADMYSFVAKEID-YANYFQTLIEVQAEYHRKSLTLLQAVLPQIKA 149
Cdd:smart00721 170 EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
PHA03247 PHA03247
large tegument protein UL36; Provisional
436-716 7.70e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 7.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  436 GSSAGRKASCAPPSMQPPAPPSELAAPLPSPLPEQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPG 515
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  516 SIQGTPCPGTQLGP------QPAASPSQLPADQSPHTLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQPSPVslsptppst 589
Cdd:PHA03247  2868 SRSPAAKPAAPARPpvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR--------- 2938
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  590 pspyglsyPPGYSMASGQLSPASAPPLASPSVFTSTLAKSRpTPKPRQRptlPPPQPPSVSLSASSPQSTEHPMLDGMSp 669
Cdd:PHA03247  2939 --------PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR-VAVPRFR---VPQPAPSREAPASSTPPLTGHSLSRVS- 3005
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720365289  670 geSMSTDL-VHFDVPSIHIELGSTLRLSP-LEHARRHSA--TDKRDSEEES 716
Cdd:PHA03247  3006 --SWASSLaLHEETDPPPVSLKQTLWPPDdTEDSDADSLfdSDSERSDLEA 3054
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
461-637 7.84e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 461 APLPSPLPEQVPDSPATPAPALSPSGASLQPTP--ERPSVSKSKELSPGSG-QKGSPGSIQGTPCPGTQLGPQPAASPsq 537
Cdd:pfam03154 180 AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPatSQPPNQTQSTAAPHTLiQQTPTLHPQRLPSPHPPLQPMTQPPP-- 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 538 lPADQSPHTLRKVSKKvAPIPPKVPFVQPGTVSDQPVGQPSPvslsptppstpspyglsYPPGYSMASGQLSPASAPPLA 617
Cdd:pfam03154 258 -PSQVSPQPLPQPSLH-GQMPPMPHSLQTGPSHMQHPVPPQP-----------------FPLTPQSSQSQVPPGPSPAAP 318
                         170       180
                  ....*....|....*....|
gi 1720365289 618 SPSVFTSTLAKSRPTPKPRQ 637
Cdd:pfam03154 319 GQSQQRIHTPPSQSQLQSQQ 338
 
Name Accession Description Interval E-value
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
1-167 1.78e-112

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 2 (Rich2) is a Rho GTPase activating protein that interacts with CD317, a lipid raft-associated integral membrane protein. It plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. Rich2 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153303  Cd Length: 248  Bit Score: 340.10  E-value: 1.78e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAG 80
Cdd:cd07619    82 MLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQSSKSSGLSSNLQPTG 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  81 AKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSF 160
Cdd:cd07619   162 AKADALREEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELLQSVLPQIKAHQEAWVEKPSY 241

                  ....*..
gi 1720365289 161 GKPLEEH 167
Cdd:cd07619   242 GKPLEEH 248
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
156-356 7.99e-102

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: 310.54  E-value: 7.99e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 156 EKPSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVV--DVQEYSADPHAIAGA 233
Cdd:cd04386     1 EKPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFslPLDEFYSDPHAVASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 234 LKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVL 313
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720365289 314 GPNLLWPQSEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEI 356
Cdd:cd04386   161 APNLLWAKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGEV 203
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
1-167 9.86e-74

The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation.


Pssm-ID: 153279 [Multi-domain]  Cd Length: 244  Bit Score: 238.77  E-value: 9.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLssslQPAG 80
Cdd:cd07595    82 VLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDSARSRYNAAHKSSGG----QGAA 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  81 AKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSF 160
Cdd:cd07595   158 AKVDALKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLPELQEQIEQSPSKPVF 237

                  ....*..
gi 1720365289 161 GKPLEEH 167
Cdd:cd07595   238 GQPLEEH 244
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
1-167 2.02e-73

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation.


Pssm-ID: 153302  Cd Length: 246  Bit Score: 238.01  E-value: 2.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAg 80
Cdd:cd07618    82 MLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSARGRYNQAHKSSGTNFQAMPS- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  81 aKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSF 160
Cdd:cd07618   161 -KIDMLKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEKVLPEIQAHQDKWMEKPAF 239

                  ....*..
gi 1720365289 161 GKPLEEH 167
Cdd:cd07618   240 GTPLEEH 246
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
173-348 1.76e-59

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: 198.26  E-value: 1.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  173 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYS-ADPHAIAGALKSYLRELPEPLMTFELY 251
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSeYDVHDVAGLLKLFLRELPEPLITYELY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  252 DEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSEGNITEMMT 331
Cdd:smart00324  81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160
                          170
                   ....*....|....*..
gi 1720365289  332 TvslQIVGIIEPIIQHA 348
Cdd:smart00324 161 R---HQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
178-347 6.76e-56

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: 188.28  E-value: 6.76e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 178 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQA 257
Cdd:cd00159     3 IIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFIEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 258 SNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSEgniTEMMTTVSLQI 337
Cdd:cd00159    83 AKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDS---DDELLEDIKKL 159
                         170
                  ....*....|
gi 1720365289 338 VGIIEPIIQH 347
Cdd:cd00159   160 NEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
177-322 2.00e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 183.52  E-value: 2.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 177 FPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-VVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWI 255
Cdd:pfam00620   2 LIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGpDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEFI 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720365289 256 QASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQS 322
Cdd:pfam00620  82 EAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-322 2.31e-37

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: 138.24  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLMISGREIAFP--IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSaDPHAIAGALKS 236
Cdd:cd04404     6 FGVSLQFLKEKNPEQEPIPpvVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEpVDFDQYE-DVHLPAVILKT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 237 YLRELPEPLMTFELYDEWIQASNIQEQDkRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPN 316
Cdd:cd04404    85 FLRELPEPLLTFDLYDDIVGFLNVDKEE-RVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPN 163

                  ....*.
gi 1720365289 317 LLWPQS 322
Cdd:cd04404   164 LLWAKD 169
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
1-149 1.90e-35

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 134.00  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAeVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPag 80
Cdd:pfam03114  93 ALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKSSKAKDES-- 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  81 akadALREEMEEAANRVEICRDQLSADMYSFVAKEIDY-ANYFQTLIEVQAEYHRKSLTLLQAVLPQIKA 149
Cdd:pfam03114 170 ----QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFvVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
159-352 2.74e-35

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


Pssm-ID: 239860  Cd Length: 196  Bit Score: 132.52  E-value: 2.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 159 SFGKPLEEHLMISGRE-IAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL-----DCCVVDvqEYSADPHAIAG 232
Cdd:cd04395     1 TFGVPLDDCPPSSENPyVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELnrggfDIDLQD--PRWRDVNVVSS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 233 ALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIV 312
Cdd:cd04395    79 LLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720365289 313 LGPNLLWPqSEGNITEMMTTVSLQiVGIIEPIIQHADWFF 352
Cdd:cd04395   159 FGPTLVRT-SDDNMETMVTHMPDQ-CKIVETLIQHYDWFF 196
BAR smart00721
BAR domain;
1-149 5.32e-35

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 132.89  E-value: 5.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289    1 MLKLCGETEDKLAQELIHFeLQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTskssgLSSSLQPAG 80
Cdd:smart00721  96 ALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA-----KKSKEKKKD 169
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   81 AKADALREEMEEAANRVEICRDQLSADMYSFVAKEID-YANYFQTLIEVQAEYHRKSLTLLQAVLPQIKA 149
Cdd:smart00721 170 EKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-352 1.67e-33

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: 127.13  E-value: 1.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDV-----QEYSADPHAIAGAL 234
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVllispEDYESDIHSVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 235 KSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLG 314
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720365289 315 PNLLwPQSEGNITEMmttvSLQIVgIIEPIIQHADWFF 352
Cdd:cd04398   161 PTLM-NAAPDNAADM----SFQSR-VIETLLDNAYQIF 192
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
190-345 3.71e-33

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: 126.01  E-value: 3.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 190 GMQEEGLFRVAPSASKLKKLKAALDCCV--VDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRL 267
Cdd:cd04377    30 GLYTEGIYRKSGSANKIKELRQGLDTDPdsVNLEDYPI--HVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERV 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720365289 268 QALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSEGNITEMMTTVSLQiVGIIEPII 345
Cdd:cd04377   108 RALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRCPDTADPLQSLQDVSKT-TTCVETLI 184
BAR_SH3BP1 cd07620
The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are ...
2-148 1.81e-32

The Bin/Amphiphysin/Rvs (BAR) domain of SH3-domain Binding Protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. SH3-domain binding protein 1 (SH3BP1 or 3BP-1) is a Rac GTPase activating protein that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. SH3BP1 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153304  Cd Length: 257  Bit Score: 126.21  E-value: 1.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   2 LKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAGA 81
Cdd:cd07620    83 LEMCCFMQNMLANILADFEMKVEKDVLQPLNKLSEEDLPEILKNKKQFAKLTTDWNSAKSRSPQAAGRSPRSGGRSEEVG 162
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720365289  82 ---------KADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIK 148
Cdd:cd07620   163 ehqgirranKGEPLKEEEEECWRKLEQCKDQYSADLYHFATKEDSYANYFIRLLELQAEYHKNSLEFLDKNITELK 238
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
160-351 3.18e-32

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: 123.71  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLMIS---GREIAfPI--EACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGAL 234
Cdd:cd04390     3 FGQRLEDTVAYErkfGPRLV-PIlvEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 235 KSYLRELPEPLMTFELYDEWIQASNI--QEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIV 312
Cdd:cd04390    82 KLYLRELPEPVIPWAQYEDFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATV 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720365289 313 LGPNLLWPQSEGNITEMMTTVSLQIVGIIEpIIQHADWF 351
Cdd:cd04390   162 FGPNILRPKVEDPATIMEGTPQIQQLMTVM-ISKHEPLF 199
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
179-347 3.21e-32

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: 124.04  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 179 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL------DCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYD 252
Cdd:cd04374    32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktsTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 253 EWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSEgNITEMMTT 332
Cdd:cd04374   112 DFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEE-TVAAIMDI 190
                         170
                  ....*....|....*
gi 1720365289 333 VSLQIVgiIEPIIQH 347
Cdd:cd04374   191 KFQNIV--VEILIEN 203
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
174-352 8.04e-32

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 122.63  E-value: 8.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 174 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDV-QEYSADPHAIAGALKSYLRELPEPLMTFEL 250
Cdd:cd04372    15 QRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDrdGEKADIsATVYPDINVITGALKLYFRDLPIPVITYDT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 251 YDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPqSEGNITEMM 330
Cdd:cd04372    95 YPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRP-PEDSALTTL 173
                         170       180
                  ....*....|....*....|..
gi 1720365289 331 TTVSLQIVgIIEPIIQHADWFF 352
Cdd:cd04372   174 NDMRYQIL-IVQLLITNEDVLF 194
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
178-339 1.27e-31

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: 121.64  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 178 PIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEWIQ 256
Cdd:cd04402    18 PILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVeVDLKAEPV--LLLASVLKDFLRNIPGSLLSSDLYEEWMS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 257 ASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWP------QSEGN----- 325
Cdd:cd04402    96 ALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPpasselQNEDLkkvts 175
                         170
                  ....*....|....
gi 1720365289 326 ITEMMTTVSLQIVG 339
Cdd:cd04402   176 LVQFLIENCQEIFG 189
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
190-329 1.30e-30

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: 118.94  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 190 GMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQA 269
Cdd:cd04407    30 GLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQA 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720365289 270 LWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL-WPQSEGNITEM 329
Cdd:cd04407   110 IYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLrCPDSSDPLTSM 170
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
179-341 7.98e-29

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


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 113.64  E-value: 7.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 179 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKaaldcCVVDVQEYSA-------DPHAIAGALKSYLRELPEPLMTFELY 251
Cdd:cd04403    20 VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLR-----FAVDHDEKLDlddskweDIHVITGALKLFFRELPEPLFPYSLF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 252 DEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSE-GNITEMM 330
Cdd:cd04403    95 NDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLRPEQEtGNIAVHM 174
                         170
                  ....*....|.
gi 1720365289 331 TTVSlQIVGII 341
Cdd:cd04403   175 VYQN-QIVELI 184
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
158-347 1.61e-28

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: 112.98  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 158 PSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEeGLFRVAPSASKLKKLKAALD---CCVVDVQEYSADPHAIAGAL 234
Cdd:cd04384     1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDseqIPDLTKDVYIQDIHSVSSLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 235 KSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLG 314
Cdd:cd04384    80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720365289 315 PNLLW-PQSEG---NITEMMTTVSLQIVgIIEPIIQH 347
Cdd:cd04384   160 PNLLRsKQIESacfSGTAAFMEVRIQSV-VVEFILNH 195
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-346 4.95e-28

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: 111.39  E-value: 4.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEhLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYSADPHAIAGALKSYL 238
Cdd:cd04373     1 FGVPLAN-VVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQdHNLDLVSKDFTVNAVAGALKSFF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 239 RELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 318
Cdd:cd04373    80 SELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLM 159
                         170       180
                  ....*....|....*....|....*...
gi 1720365289 319 WPQSEgNITEMMTTVSLQIvgIIEPIIQ 346
Cdd:cd04373   160 RPDFT-SMEALSATRIYQT--IIETFIQ 184
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
160-317 5.55e-28

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: 111.30  E-value: 5.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLMIS-----GREIAFPIEACVTMLLECG-MQEEGLFRVAPSASKLKKLKAALDCCV-VDVQEYSA--DPHAI 230
Cdd:cd04400     2 FGSPLEEAVELSshkynGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYdVDLFSSSLypDVHTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 231 AGALKSYLRELPEPLMTFELYDEWIQASNIQEQD-KRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNM 309
Cdd:cd04400    82 AGLLKLYLRELPTLILGGELHNDFKRLVEENHDRsQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNV 161

                  ....*...
gi 1720365289 310 AIVLGPNL 317
Cdd:cd04400   162 CIVFSPTL 169
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
179-347 1.01e-26

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: 107.39  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 179 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQ----EYSadPHAIAGALKSYLRELPEPLMTFELYDEW 254
Cdd:cd04385    19 VDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQlregEYT--VHDVADVLKRFLRDLPDPLLTSELHAEW 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 255 IQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQsegnitEMMTTVS 334
Cdd:cd04385    97 IEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTD------EHSVGQT 170
                         170
                  ....*....|...
gi 1720365289 335 LQIVGIIEPIIQH 347
Cdd:cd04385   171 SHEVKVIEDLIDN 183
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
179-337 1.99e-25

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: 104.24  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 179 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEY--SADPHAIAGALKSYLRELPEPLMTFELYDEWIQ 256
Cdd:cd04387    20 VRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMlsEMDVNAIAGTLKLYFRELPEPLFTDELYPNFAE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 257 ASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWP---QSEGNITEMMTTV 333
Cdd:cd04387   100 GIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPsekESKIPTNTMTDSW 179

                  ....
gi 1720365289 334 SLQI 337
Cdd:cd04387   180 SLEV 183
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
174-327 4.45e-25

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: 103.27  E-value: 4.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 174 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC--CVVDVQEYSadPHAIAGALKSYLRELPEPLMTFELY 251
Cdd:cd04378    15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENgkDLVELSELS--PHDISSVLKLFLRQLPEPLILFRLY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 252 DEWIQ-ASNIQ---EQDKR----------LQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNL 317
Cdd:cd04378    93 NDFIAlAKEIQrdtEEDKApntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTL 172
                         170
                  ....*....|.
gi 1720365289 318 LWP-QSEGNIT 327
Cdd:cd04378   173 IRPrPGDADVS 183
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-329 2.66e-24

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: 101.01  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLE----EHLMISGREIAFPIEACVTmlLECGMQEEGLFRVAPSASKLKKLKAALD---CCVvdvqeYSADPHAIAG 232
Cdd:cd04394     2 FGVPLHslphSTVPEYGNVPKFLVDACTF--LLDHLSTEGLFRKSGSVVRQKELKAKLEggeACL-----SSALPCDVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 233 ALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIV 312
Cdd:cd04394    75 LLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVI 154
                         170
                  ....*....|....*..
gi 1720365289 313 LGPNLLwpQSEGNITEM 329
Cdd:cd04394   155 FAPNLF--QSEEGGEKM 169
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
179-356 8.39e-24

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


Pssm-ID: 239841  Cd Length: 206  Bit Score: 99.82  E-value: 8.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 179 IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQAS 258
Cdd:cd04376    13 VESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAFIGTA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 259 NIQEQDkRLQALWNACEKLPKANHNNIKYLIKFLSKLSEY-QDV----------NKMTPSNMAIVLGPNLLWPQ----SE 323
Cdd:cd04376    93 LLEPDE-QLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHaADSidedgqevsgNKMTSLNLATIFGPNLLHKQksgeRE 171
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720365289 324 GNITEMMTTVSLQIVGIIEPIIQHADWFF--PGEI 356
Cdd:cd04376   172 FVQASLRIEESTAIINVVQTMIDNYEELFmvSPEL 206
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-325 1.60e-23

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: 99.34  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLM-----ISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDVQEYSADPHAIAG 232
Cdd:cd04391     2 FGVPLSTLLErdqkkVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEakFYEGTFLWDQVKQHDAAS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 233 ALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIV 312
Cdd:cd04391    82 LLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMI 161
                         170
                  ....*....|...
gi 1720365289 313 LGPNLLWPQSEGN 325
Cdd:cd04391   162 MAPNLFPPRGKHS 174
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-325 2.90e-23

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: 98.59  E-value: 2.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLE---------EHLMISGREIAFP--IEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSAD-P 227
Cdd:cd04397     1 FGVPLEilvekfgadSTLGVGPGKLRIPalIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKEnP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 228 HAIAGALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDV-----N 302
Cdd:cd04397    81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgS 160
                         170       180
                  ....*....|....*....|...
gi 1720365289 303 KMTPSNMAIVLGPNLLWPQSEGN 325
Cdd:cd04397   161 KMDIHNLATVITPNILYSKTDNP 183
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
160-318 1.75e-22

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: 95.57  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL---DCCVVDVQEYSaDPHAIAGALKS 236
Cdd:cd04383     3 FNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFergEDPLADDQNDH-DINSVAGVLKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 237 YLRELPEPLMTFELYD---EWIQASNIQEQDKRLQALwnaCEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVL 313
Cdd:cd04383    82 YFRGLENPLFPKERFEdlmSCVKLENPTERVHQIREI---LSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICF 158

                  ....*
gi 1720365289 314 GPNLL 318
Cdd:cd04383   159 GPTLM 163
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
173-318 7.87e-22

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: 93.53  E-value: 7.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 173 REIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYD 252
Cdd:cd04406    13 RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYE 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720365289 253 EWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 318
Cdd:cd04406    93 EFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-321 1.68e-21

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 93.33  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC--VVDVQEYSadPHAIAGALKSY 237
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGkdLVELSELS--PHDISNVLKLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 238 LRELPEPLMTFELYDEWIQ-ASNIQEQDKRLQALWNACEK---------------------LPKANHNNIKYLIKFLSKL 295
Cdd:cd04409    79 LRQLPEPLILFRLYNEFIGlAKESQHVNETQEAKKNSDKKwpnmctelnrillkskdllrqLPAPNYNTLQFLIVHLHRV 158
                         170       180
                  ....*....|....*....|....*.
gi 1720365289 296 SEYQDVNKMTPSNMAIVLGPNLLWPQ 321
Cdd:cd04409   159 SEQAEENKMSASNLGIIFGPTLIRPR 184
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
158-317 2.46e-21

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: 92.14  E-value: 2.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 158 PSFGKPLEE--HLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALK 235
Cdd:cd04393     1 KVFGVPLQElqQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 236 SYLRELPEPLMTFELYDEWIQ----ASNIQEQDKRLQALwnaCEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAI 311
Cdd:cd04393    81 LFLQELPEGLIPASLQIRLMQlyqdYNGEDEFGRKLRDL---LQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAA 157

                  ....*.
gi 1720365289 312 VLGPNL 317
Cdd:cd04393   158 VFGPDV 163
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
160-317 3.50e-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: 91.34  E-value: 3.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPL----EEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYsaDPHAIAGAL 234
Cdd:cd04381     1 FGASLslavERSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRrESPNLEEY--EPPTVASLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 235 KSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLG 314
Cdd:cd04381    79 KQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLS 158

                  ...
gi 1720365289 315 PNL 317
Cdd:cd04381   159 PTV 161
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
182-317 4.89e-20

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: 88.50  E-value: 4.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 182 CVTMLLECGMQEEGLFRVAPSASKLKKL-------KAALDCCVVDVqeysadpHAIAGALKSYLRELPEPLMTFELYDEW 254
Cdd:cd04382    24 CVNEIEARGLTEEGLYRVSGSEREVKALkekflrgKTVPNLSKVDI-------HVICGCLKDFLRSLKEPLITFALWKEF 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720365289 255 IQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEyQDVNKMTPSNMAIVLGPNL 317
Cdd:cd04382    97 MEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQ-SPECKMDINNLARVFGPTI 158
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
174-327 5.91e-20

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: 88.72  E-value: 5.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 174 EIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDC--CVVDVQEYSadPHAIAGALKSYLRELPEPLMTFELY 251
Cdd:cd04408    15 EVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENgrDLVDLSGHS--PHDITSVLKHFLKELPEPVLPFQLY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 252 DEWIQ-ASNIQEQDKR-----------LQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLW 319
Cdd:cd04408    93 DDFIAlAKELQRDSEKaaespsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLR 172

                  ....*...
gi 1720365289 320 PQSEGNIT 327
Cdd:cd04408   173 PLVGGDVS 180
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
160-323 1.74e-19

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


Pssm-ID: 239854  Cd Length: 187  Bit Score: 86.68  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEhLMISGREiAFP---IEACVTMLLEC-----GMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSaDPHAIA 231
Cdd:cd04389     1 FGSSLEE-IMDRQKE-KYPelkLPWILTFLSEKvlalgGFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGLE-DPHVPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 232 GALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLqalwnaCEKLPKANHNNIKYLIKFLSKLSEYQDV--NKMTPSNM 309
Cdd:cd04389    78 SLLKLWLRELEEPLIPDALYQQCISASEDPDKAVEI------VQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNL 151
                         170
                  ....*....|....
gi 1720365289 310 AIVLGPNLLWPQSE 323
Cdd:cd04389   152 AMVFAPNILRCTSD 165
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
1-146 7.81e-19

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


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 85.19  E-value: 7.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   1 MLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAg 80
Cdd:cd07307    55 ALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLAEA- 133
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720365289  81 akadalREEMEEAANRVEICRDQLSADMYSFVA-KEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQ 146
Cdd:cd07307   134 ------EEELQEAKEKYEELREELIEDLNKLEEkRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
156-317 1.58e-18

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 84.78  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 156 EKPSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALD--CCVVDVQEYSAdpHAIAGA 233
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIEssTDNVNYDGQQA--YDVADM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 234 LKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVL 313
Cdd:cd04375    79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCL 158

                  ....
gi 1720365289 314 GPNL 317
Cdd:cd04375   159 APSL 162
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
160-338 6.65e-18

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: 82.89  E-value: 6.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPL--EEHLMISgREIAFpieacvtmlLECGMQEEGLFRVAPSASKLKKLKAALDC-CVVDVQEYSADPHAIAGALKS 236
Cdd:cd04392     1 FGAPLteEGIAQIY-QLIEY---------LEKNLRVEGLFRKPGNSARQQELRDLLNSgTDLDLESGGFHAHDCATVLKG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 237 YLRELPEPLMTFELY------------DEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKM 304
Cdd:cd04392    71 FLGELPEPLLTHAHYpahlqiadlcqfDEKGNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKM 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720365289 305 TPSNMAIVLGPNLLWPQS------EGNITEMMTTVSLQIV 338
Cdd:cd04392   151 SADNLALLFTPHLICPRNltpedlHENAQKLNSIVTFMIK 190
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
160-323 1.55e-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: 78.66  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEE--HLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAAL--DCCVVDVQEYS-ADPHAIAGAL 234
Cdd:cd04379     1 FGVPLSRlvEREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFerNSAAVELSEELyPDINVITGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 235 KSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNA---CEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAI 311
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTlsiIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                         170
                  ....*....|..
gi 1720365289 312 VLGPNLLWPQSE 323
Cdd:cd04379   161 CFGPVLMFCSQE 172
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
160-351 3.81e-12

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


Pssm-ID: 239861  Cd Length: 225  Bit Score: 66.28  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 160 FGKPLEEHLMISGREIAF-------------PI--EACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCC-----VVD 219
Cdd:cd04396     2 FGVSLEESLKYASVAISIvdedgeqyvygyiPVvvAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPpdygkSFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 220 VQEYSAdpHAIAGALKSYLRELPEPLMTFELYDEW-----------------IQASNIQEQDKRLQALWNACEKLPKANH 282
Cdd:cd04396    82 WDGYTV--HDAASVLRRYLNNLPEPLVPLDLYEEFrnplrkrprilqymkgrINEPLNTDIDQAIKEYRDLITRLPNLNR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 283 NNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLW-PQSEGNITEMMTTVSlqivgIIEPIIQHADWF 351
Cdd:cd04396   160 QLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILShPDHEMDPKEYKLSRL-----VVEFLIEHQDKF 224
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
186-318 8.86e-10

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: 59.28  E-value: 8.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 186 LLECGMQEEGLFR----VAPSASKLKKLKAALDCCVVDVQeySADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQ 261
Cdd:cd04380    61 LYTRGLAQEGLFEepglPSEPGELLAEIRDALDTGSPFNS--PGSAESVAEALLLFLESLPDPIIPYSLYERLLEAVANN 138
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720365289 262 EQDKRlQALWNAcekLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 318
Cdd:cd04380   139 EEDKR-QVIRIS---LPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLL 191
PHA03247 PHA03247
large tegument protein UL36; Provisional
436-716 7.70e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 7.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  436 GSSAGRKASCAPPSMQPPAPPSELAAPLPSPLPEQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPG 515
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  516 SIQGTPCPGTQLGP------QPAASPSQLPADQSPHTLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQPSPVslsptppst 589
Cdd:PHA03247  2868 SRSPAAKPAAPARPpvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR--------- 2938
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  590 pspyglsyPPGYSMASGQLSPASAPPLASPSVFTSTLAKSRpTPKPRQRptlPPPQPPSVSLSASSPQSTEHPMLDGMSp 669
Cdd:PHA03247  2939 --------PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR-VAVPRFR---VPQPAPSREAPASSTPPLTGHSLSRVS- 3005
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720365289  670 geSMSTDL-VHFDVPSIHIELGSTLRLSP-LEHARRHSA--TDKRDSEEES 716
Cdd:PHA03247  3006 --SWASSLaLHEETDPPPVSLKQTLWPPDdTEDSDADSLfdSDSERSDLEA 3054
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
2-143 4.61e-06

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. The BAR domains of endophilin-A1 and A3 form crescent-shaped dimers that can detect membrane curvature and drive membrane bending.


Pssm-ID: 153276  Cd Length: 223  Bit Score: 48.46  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   2 LKLCGETEDKLAQelIHFELQ--VERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqtskssglssslqpa 79
Cdd:cd07592    90 LVEVGEALKQLAE--VKDSLDdnVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDYDYKKRK----------------- 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720365289  80 GAKA--DALREEMEEAANRVEICrdqlSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAV 143
Cdd:cd07592   151 QGKGpdEELKQAEEKFEESKELA----ENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILEEL 212
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
190-318 5.06e-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: 47.95  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 190 GMQEEGLFRvAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQ-ASNIQEQDKRLQ 268
Cdd:cd04388    30 GLESSTLYR-TQSSSSLTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMISrAQEVQSSDEYAQ 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720365289 269 ALWNA--CEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLL 318
Cdd:cd04388   109 LLRKLirSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLF 160
PRK10263 PRK10263
DNA translocase FtsK; Provisional
462-580 6.12e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.70  E-value: 6.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  462 PLPSPLPEQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQLGP-QPAASPSQLPA 540
Cdd:PRK10263   371 PVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPeQPVAGNAWQAE 450
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720365289  541 DQSPH-----TLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQPSPV 580
Cdd:PRK10263   451 EQQSTfapqsTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPV 495
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
6-148 8.61e-06

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A2 (or endophilin-2) is also referred to as SH3P8 (SH3 domain containing protein 8) or SH3GL1 (SH3 domain containing Grb2-like protein 1). It localizes to presynaptic nerve terminals and forms heterodimers with endophilin-A1 through their BAR domains. Endophilin-A2 binds dynamin 1, synaptojanin 1, and the beta1-adrenergic receptor cytoplasmic tail through its SH3 domain.


Pssm-ID: 153298  Cd Length: 223  Bit Score: 47.40  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   6 GETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqtskssglssslqpAGAKADa 85
Cdd:cd07614    94 GESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDFDYKKKR----------------QGKIPD- 156
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720365289  86 lrEEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIK 148
Cdd:cd07614   157 --EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLK 217
PHA03247 PHA03247
large tegument protein UL36; Provisional
460-662 1.51e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  460 AAPLPSPLPEQVPD-SPATPAPALSPSGASLQPTPERPSVSkskelsPGSGQKGSPGSIQGTPCPGTQLGPQPAAS--PS 536
Cdd:PHA03247  2552 PPPLPPAAPPAAPDrSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPRAPVDDRGDPRGPAPPSPLPPDThaPD 2625
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  537 QLPADQSPHTLRKVSKKVAPIPPKvpfvqpgtvsDQPVGQPSP--VSLSPTPPSTPSPYGLSYPPgysmaSGQLSPASAP 614
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPPPTVPPP----------ERPRDDPAPgrVSRPRRARRLGRAAQASSPP-----QRPRRRAARP 2690
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1720365289  615 PLASPSVFTSTLAKSR-PTPKPRQRPTLPPPQPPSVSLSASSPQSTEHP 662
Cdd:PHA03247  2691 TVGSLTSLADPPPPPPtPEPAPHALVSATPLPPGPAAARQASPALPAAP 2739
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
6-141 1.63e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins localized at synapses that interacts with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A3 (or endophilin-3) is also referred to as SH3P13 (SH3 domain containing protein 13) or SH3GL3 (SH3 domain containing Grb2-like protein 3). It regulates Arp2/3-dependent actin filament assembly during endocytosis. It binds N-WASP through its SH3 domain and enhances the ability of N-WASP to activate the Arp2/3 complex. Endophilin-A3 co-localizes with the vesicular glutamate transporter 1 (VGLUT1), and may play an important role in the synaptic release of glutamate.


Pssm-ID: 153299  Cd Length: 223  Bit Score: 46.55  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   6 GETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqtskssglssslqpAGAKADa 85
Cdd:cd07615    94 GESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFDYKKKR----------------QGKIPD- 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720365289  86 lrEEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQ 141
Cdd:cd07615   157 --EEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILE 210
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
6-148 5.46e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 45.00  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   6 GETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRwqqtskssglssslqpAGAKADa 85
Cdd:cd07613    94 GEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKR----------------QGKIPD- 156
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720365289  86 lrEEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIK 148
Cdd:cd07613   157 --EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQVTVKLE 217
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
461-637 7.84e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 461 APLPSPLPEQVPDSPATPAPALSPSGASLQPTP--ERPSVSKSKELSPGSG-QKGSPGSIQGTPCPGTQLGPQPAASPsq 537
Cdd:pfam03154 180 AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPatSQPPNQTQSTAAPHTLiQQTPTLHPQRLPSPHPPLQPMTQPPP-- 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 538 lPADQSPHTLRKVSKKvAPIPPKVPFVQPGTVSDQPVGQPSPvslsptppstpspyglsYPPGYSMASGQLSPASAPPLA 617
Cdd:pfam03154 258 -PSQVSPQPLPQPSLH-GQMPPMPHSLQTGPSHMQHPVPPQP-----------------FPLTPQSSQSQVPPGPSPAAP 318
                         170       180
                  ....*....|....*....|
gi 1720365289 618 SPSVFTSTLAKSRPTPKPRQ 637
Cdd:pfam03154 319 GQSQQRIHTPPSQSQLQSQQ 338
PHA03247 PHA03247
large tegument protein UL36; Provisional
460-670 1.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  460 AAPLPSPLPeqvPDSPATPAPALSPS---------GASLQPTPERPS-------VSKSKELSPGSGQKGSPGSIQG---- 519
Cdd:PHA03247  2610 GPAPPSPLP---PDTHAPDPPPPSPSpaanepdphPPPTVPPPERPRddpapgrVSRPRRARRLGRAAQASSPPQRprrr 2686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  520 --------------TPCPGTQLGPQPAASPSQLPADQSPHTLRKVSKK--VAPIPPKVPFVQPGTVSDQPVGQPS----- 578
Cdd:PHA03247  2687 aarptvgsltsladPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAlpAAPAPPAVPAGPATPGGPARPARPPttagp 2766
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  579 PVSLSPTPPSTPSPYGLSYPPGYSMASGQLS-PASAPPLASPSVFTSTLAKSRPTPKPRQRPTLPPPQPPSVSLSASSPQ 657
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESlPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846
                          250
                   ....*....|...
gi 1720365289  658 STEHPMLDGMSPG 670
Cdd:PHA03247  2847 PPSLPLGGSVAPG 2859
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
5-147 1.49e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle.


Pssm-ID: 153278  Cd Length: 229  Bit Score: 43.92  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289   5 CGETEDKLAQ---ELIHfelQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSsslqpaga 81
Cdd:cd07594    98 VGQAQKKLGQaerEFIQ---TSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDACKTRVKKAKSAEAIE-------- 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  82 KADA-LREEMEEAANRVEICRDQLSADMYSFvakeidyANYFQTL---IEVQAEYHRKSLTLLQAVLPQI 147
Cdd:cd07594   167 QAEQdLRVAQSEFDRQAEITKLLLEGISSTH-------ANHLRCLrdfVEAQMTYYAQCYQYMDDLQRQL 229
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
436-638 1.79e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 436 GSSAGRKASCAPPSMQPPAPPSELAAPLPSPLPEQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPG 515
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAP 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 516 SIQGTPCPGTQLGPQPAASPSQLPADQSPHTLRKVSKKVAPIPPKVPfvqpgTVSDQPVGQPSPVSLSPTPPSTPSPYGL 595
Cdd:PRK12323  451 APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP-----PWEELPPEFASPAPAQPDAAPAGWVAES 525
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720365289 596 SYPPGYSMASGQLSPASAPPLASPSvftstlaksrPTPKPRQR 638
Cdd:PRK12323  526 IPDPATADPDDAFETLAPAPAAAPA----------PRAAAATE 558
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
458-658 1.81e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  458 ELAAPLPSPLPEQVPDSPATPAPA--------LSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSIQG--TPCPGTQL 527
Cdd:PHA03307   181 ETARAPSSPPAEPPPSTPPAAASPrpprrsspISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGpeNECPLPRP 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  528 GPQPAASPSQLPADQSPHTLRKVS-KKVAPIPPKVPFVQPGTVSDQPVGQPSPVSLSPTPPSTPspyGLSYPPGYSMASG 606
Cdd:PHA03307   261 APITLPTRIWEASGWNGPSSRPGPaSSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRES---SSSSTSSSSESSR 337
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720365289  607 QLSPASAPPLASPSvfTSTLAKSRPTPKPRQRPTLPPPQPPSVSLSASSPQS 658
Cdd:PHA03307   338 GAAVSPGPSPSRSP--SPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTR 387
PHA03247 PHA03247
large tegument protein UL36; Provisional
461-637 3.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  461 APLPSPLPEQVPDSPATPAPALSPSGASLQPTPerPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQLGPQPAASPSQLPA 540
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAP--PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP 2786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  541 DQSPHTLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQ-------PSPVSLSPTPPSTPSPYGLSYPPGYSMASG---QLSP 610
Cdd:PHA03247  2787 AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspagplpPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRP 2866
                          170       180
                   ....*....|....*....|....*..
gi 1720365289  611 ASAPPLASPSVFTSTLAKSRPTPKPRQ 637
Cdd:PHA03247  2867 PSRSPAAKPAAPARPPVRRLARPAVSR 2893
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
473-535 4.89e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 43.54  E-value: 4.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720365289 473 DSPATP-APALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQLGPQPAASP 535
Cdd:PLN02217  587 DSPSTVvAPSTSPPAGHLGSPPATPSKIVSPSTSPPASHLGSPSTTPSSPESSIKVASTETASP 650
PHA03379 PHA03379
EBNA-3A; Provisional
480-673 6.29e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 43.12  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 480 PALSPSGASLQPTPE-RPSVSKSKELSP--GSGQKGSPGSIQGT------------PCPGTQLGPQPAasPSQLPADQSP 544
Cdd:PHA03379  408 ASEPTYGTPRPPVEKpRPEVPQSLETATshGSAQVPEPPPVHDLepgplhdqhsmaPCPVAQLPPGPL--QDLEPGDQLP 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 545 HTLRKVSKKVAPIP-PKVPFVQP-------------GTVSDQPVG---QPSPVSLSPTPPSTPSPYGLSYPPGYSMASGQ 607
Cdd:PHA03379  486 GVVQDGRPACAPVPaPAGPIVRPweaslsqvpgvafAPVMPQPMPvepVPVPTVALERPVCPAPPLIAMQGPGETSGIVR 565
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720365289 608 LSPASAPPLASPSVFTST--------LAKSRPTPKPRQRptlpppqppsvSLSASSPQ----STEHPMLDGMSPGESM 673
Cdd:PHA03379  566 VRERWRPAPWTPNPPRSPsqmsvrdrLARLRAEAQPYQA-----------SVEVQPPQltqvSPQQPMEYPLEPEQQM 632
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
461-662 1.24e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 461 APLPSPLPEQVPDSPATPAPALSPSgaslQPTPERPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQlgpqPAASPSQLPA 540
Cdd:PLN03209  332 ESDAADGPKPVPTKPVTPEAPSPPI----EEEPPQPKAVVPRPLSPYTAYEDLKPPTSPIPTPPSS----SPASSKSVDA 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 541 DQSPHTLRKVSkkVAPIPPKVPFVQPGTVSDQPVGQPSPVS----LSPTPPSTPSPYGLSYPPGYSMASGQLSPASAPPL 616
Cdd:PLN03209  404 VAKPAEPDVVP--SPGSASNVPEVEPAQVEAKKTRPLSPYAryedLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPAT 481
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720365289 617 AspsvFTSTLAKSRPTPKPRQRPTLPPPQPPSVSLSASSPQSTEHP 662
Cdd:PLN03209  482 A----ATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAP 523
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
224-295 1.82e-03

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: 40.39  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720365289 224 SADPHAIAGALKSYLRELPEPLMTFELYD------EWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKL 295
Cdd:cd04399    75 KFEPSTVASVLKLYLLELPDSLIPHDIYDlirslySAYPPSQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYRL 152
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
452-684 2.25e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 452 PPAPPSELAAPLPSPLPEQVPD--SPATPAPALS-PSGASLQPTPErPSVSKSKELSPGSGQKGS-----PGSIQGTPCP 523
Cdd:pfam03154 223 STAAPHTLIQQTPTLHPQRLPSphPPLQPMTQPPpPSQVSPQPLPQ-PSLHGQMPPMPHSLQTGPshmqhPVPPQPFPLT 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 524 ---GTQLGPQPAASPSQLPADQSPHTLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQP--SPVSLSPTPPSTPSPYGLSYP 598
Cdd:pfam03154 302 pqsSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPptTPIPQLPNPQSHKHPPHLSGP 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 599 PGYSMASGQLSPASAPPLASPSVFTSTLAKSRP---TPKPRQRPTLPPPQPPSVSLSASSPQSTEHPMLDGMSPGESMST 675
Cdd:pfam03154 382 SPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPlqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSP 461

                  ....*....
gi 1720365289 676 DLVHFDVPS 684
Cdd:pfam03154 462 FPQHPFVPG 470
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
433-638 3.80e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 433 ARRGSSAGRKASCAPPSMQPPAPPSELAAPLPSPLPEQvpdsPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKG 512
Cdd:PRK07764  586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAA----PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 513 SPGSIQGTPCPGTQLGPQPAASPSQLPADQSPHTlrKVSKKVAPIPPKVPFVQPgtvSDQPVGQPSPVSLSPTPPSTPSP 592
Cdd:PRK07764  662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAG--AAPAQPAPAPAATPPAGQ---ADDPAAQPPQAAQGASAPSPAAD 736
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720365289 593 YGLSYP--PGYSMASGQLSPASAPPLASPSVFTSTLAKSRPTPKPRQR 638
Cdd:PRK07764  737 DPVPLPpePDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
460-576 3.93e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 460 AAPLPSPLPEQVPDS-PATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQLGPQPAASPSQL 538
Cdd:PRK14951  387 AAPAAAPVAQAAAAPaPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRV 466
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720365289 539 pADQSPHTLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQ 576
Cdd:PRK14951  467 -APEPAVASAAPAPAAAPAAARLTPTEEGDVWHATVQQ 503
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
460-544 3.97e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 460 AAPLPSPLPEQVPDSPATPAPALSPSGASLQPTPeRPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQLGPQPAASPSQLP 539
Cdd:PRK07764  423 PAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSP-PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPA 501

                  ....*
gi 1720365289 540 ADQSP 544
Cdd:PRK07764  502 APAGA 506
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
464-563 4.09e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289 464 PSPLP-----EQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQLGPQPAASPSQL 538
Cdd:PTZ00449  569 PSKIPtlskkPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERP 648
                          90       100
                  ....*....|....*....|....*
gi 1720365289 539 PADQSPhtlrKVSKkvAPIPPKVPF 563
Cdd:PTZ00449  649 EGPKII----KSPK--PPKSPKPPF 667
PHA03247 PHA03247
large tegument protein UL36; Provisional
432-568 4.48e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  432 VARRGSSagrKASCAPPSMQPPAPPSELAAPLPSPLPE---QVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGS 508
Cdd:PHA03247  2862 VRRRPPS---RSPAAKPAAPARPPVRRLARPAVSRSTEsfaLPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  509 gqkgSPGSIQGTPCPGTQLGPQPAASPSQLPAdQSPHTLRKVSKKVAPIPPKVPFVQPGT 568
Cdd:PHA03247  2939 ----PQPPLAPTTDPAGAGEPSGAVPQPWLGA-LVPGRVAVPRFRVPQPAPSREAPASST 2993
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
472-658 8.71e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 8.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  472 PDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSiQGTPCPGTQLGPqPAASPSQLPADQSPHTLRKVS 551
Cdd:PHA03307    61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGS-PTPPGPSSPDPP-PPTPPPASPPPSPAPDLSEML 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720365289  552 KKVAPIPPKVPFVQPGTVSDQPVGQPSPVSLSPTPPSTPSPYGLSYPPGYSMASGQLSPASAPPLASPSVFTSTLAKSRP 631
Cdd:PHA03307   139 RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASAS 218
                          170       180
                   ....*....|....*....|....*..
gi 1720365289  632 TPKPRQRPTLPPPQPPSVSLSASSPQS 658
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESS 245
 
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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