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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  455 QAHVRRCRALQGQVAEL---RAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDA 531
Cdd:TIGR02168  305 QILRERLANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                           90
                   ....*....|..
gi 1907101034  532 ERRNQLLQREME 543
Cdd:TIGR02168  385 RSKVAQLELQIA 396

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034   40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVIPFARYEDF 118
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPdLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEEF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  119 LSCAQLltKDEGEGTVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILRPQIEDPVTIMEgT 198
Cdd:smart00324  84 IEAAKL--EDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-I 160

                          170
                   ....*....|....
gi 1907101034  199 SLVQHLMTVLIRKH 212
Cdd:smart00324 161 RHQNTVIEFLIENA 174

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  455 QAHVRRCRALQGQVAEL---RAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDA 531
Cdd:TIGR02168  305 QILRERLANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                           90
                   ....*....|..
gi 1907101034  532 ERRNQLLQREME 543
Cdd:TIGR02168  385 RSKVAQLELQIA 396

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 469 AELRAELCQQRT-EYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAE---RRNQLLQREMEE 544
Cdd:pfam12718  12 AQERAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEnltRKIQLLEEELEE 91

                          90
                  ....*....|
gi 1907101034 545 FFSTLGSLTT 554
Cdd:pfam12718  92 SDKRLKETTE 101

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 462 RALQGQVAELRAELcqqrTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLR-----NSE-------RARE 529
Cdd:cd22887     7 QELEKRLAELEAEL----ASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRklqeeNDElverwmaKKQQ 82

                  ....*..
gi 1907101034 530 DAERRNQ 536
Cdd:cd22887    83 EADKMNE 89

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFARYEDFL 119
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 120 SCAQLLTKDEGEgtVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILRPQIEDPVTIMEGTS 199
Cdd:cd00159    81 ELAKIEDEEERI--EALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLEDIKK 158

                  ....*....
gi 1907101034 200 LVQHLMTVL 208
Cdd:cd00159   159 LNEIVEFLI 167

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVIPFARYEDF 118
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907101034 119 LSCAQLltKDEGEGTVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILRPQ 187
Cdd:pfam00620  81 IEAAKL--PDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  20 FGQRLEDTVHHERKFGPrlAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLK 99
Cdd:cd04404     6 FGVSLQFLKEKNPEQEP--IPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEDVHLPAVILK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 100 LYLRELPEPVIPFARYEDFLScaqlLTKDEGEGTVELAKQ-VSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATV 178
Cdd:cd04404    84 TFLRELPEPLLTFDLYDDIVG----FLNVDKEERVERVKQlLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVV 159

                  ....*....
gi 1907101034 179 FGPNILRPQ 187
Cdd:cd04404   160 FGPNLLWAK 168

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  20 FGQRLEDTVHHERKfgprLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCG-------EKPLFDSttDVH 92
Cdd:cd04398     1 FGVPLEDLILREGD----NVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDplnvlliSPEDYES--DIH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  93 TVASLLKLYLRELPEPVIPFARYEDFLSCAQLltKDEGEGTVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSV 172
Cdd:cd04398    75 SVASLLKLFFRELPEPLLTKALSREFIEAAKI--EDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSV 152

                         170
                  ....*....|..
gi 1907101034 173 QNLATVFGPNIL 184
Cdd:cd04398   153 NNLAIIWGPTLM 164

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  20 FGQRLED--TVHHERkfgprLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCG--EKPLFDST-TDVHTV 94
Cdd:cd04395     2 FGVPLDDcpPSSENP-----YVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGgfDIDLQDPRwRDVNVV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  95 ASLLKLYLRELPEPVIPFARYEDFLSCAQLltKDEGEGTVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQN 174
Cdd:cd04395    77 SSLLKSFFRKLPEPLFTNELYPDFIEANRI--EDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRN 154

                         170       180
                  ....*....|....*....|.
gi 1907101034 175 LATVFGPNILRPQiEDPVTIM 195
Cdd:cd04395   155 LAIVFGPTLVRTS-DDNMETM 174

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTT--DVHTVASLLKLYLRELPEPVIPFARYED 117
Cdd:cd04383    19 PLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNdhDINSVAGVLKLYFRGLENPLFPKERFED 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907101034 118 FLSCAQLltKDEGEGTVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILR-PQIEDPV 192
Cdd:cd04383    99 LMSCVKL--ENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPvPEGQDQV 172

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDC-GEKPLFDSTT--DVHTVASLLKLYLRELPEPVIPFARYE 116
Cdd:cd04372    17 PMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdGEKADISATVypDINVITGALKLYFRDLPIPVITYDTYP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 117 DFLSCAQLLTKDEGEGTVELAkqVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILRPQIEDPVTIME 196
Cdd:cd04372    97 KFIDAAKISNPDERLEAVHEA--LMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALTTLN 174

                         170       180
                  ....*....|....*....|
gi 1907101034 197 GTSLVQHLMTVLIRKHGQLF 216
Cdd:cd04372   175 DMRYQILIVQLLITNEDVLF 194

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  20 FGQRLEDTVHHERKFGPRLA-PLLVEQCVDFIRE-RGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLfDSTTDVHTVASL 97
Cdd:cd04389     1 FGSSLEEIMDRQKEKYPELKlPWILTFLSEKVLAlGGFQTEGIFRVPGDIDEVNELKLRVDQWDYPL-SGLEDPHVPASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  98 LKLYLRELPEPVIPFARYEDFLScaqllTKDEGEGTVELakqVSNLPQANYNLLRYICKFLDEVQAHSDV--NKMSVQNL 175
Cdd:cd04389    80 LKLWLRELEEPLIPDALYQQCIS-----ASEDPDKAVEI---VQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNL 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907101034 176 ATVFGPNILRPQIEDPVTIMEGTSLVQHLMTVLI 209
Cdd:cd04389   152 AMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLI 185

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  32 RKFgPRLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGeKPLFD-STTDVHTVASLLKLYLRELPEPVI 110
Cdd:cd04378    10 RDF-PDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENG-KDLVElSELSPHDISSVLKLFLRQLPEPLI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 111 PFARYEDFLSCAQLLTKDEGEGT------------VELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATV 178
Cdd:cd04378    88 LFRLYNDFIALAKEIQRDTEEDKapntpievnriiRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIV 167

                         170       180
                  ....*....|....*....|....
gi 1907101034 179 FGPNILRP-QIEDPVTImegTSLV 201
Cdd:cd04378   168 FGPTLIRPrPGDADVSL---SSLV 188

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFARYEDFL 119
Cdd:cd04407    16 PIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDFL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 120 SCAQLLTKDEGEGTVelAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILR-PQIEDPVTIMEGT 198
Cdd:cd04407    96 RAVELPEKQEQLQAI--YRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRcPDSSDPLTSMKDV 173

                         170
                  ....*....|...
gi 1907101034 199 SLVQHLMTVLIRK 211
Cdd:cd04407   174 AKTTTCVEMLIKE 186

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGE---KPLFDSTTDVHTVASLLKLYLRELPEPVIPFARYE 116
Cdd:cd04396    33 PVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPdygKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLYE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 117 DF---------------LSCAQLLTKDEGEGTVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGP 181
Cdd:cd04396   113 EFrnplrkrprilqymkGRINEPLNTDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQP 192

                  ...
gi 1907101034 182 NIL 184
Cdd:cd04396   193 GIL 195

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSF--DCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFARYED 117
Cdd:cd04385    16 PVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 118 FLSCAQLLTKDEGegtVELAKQV-SNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILRPQIEDPVTIME 196
Cdd:cd04385    96 WIEAAELENKDER---IARYKELiRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDEHSVGQTSH 172

                         170
                  ....*....|
gi 1907101034 197 GTSLVQHLMT 206
Cdd:cd04385   173 EVKVIEDLID 182

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  40 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFARYEDFL 119
Cdd:cd04409    17 PFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEFI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034 120 SCAQ------------LLTKDEGEGT--------VELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVF 179
Cdd:cd04409    97 GLAKesqhvnetqeakKNSDKKWPNMctelnrilLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGIIF 176

                         170       180
                  ....*....|....*....|....*
gi 1907101034 180 GPNILRP-QIEDPVTImegTSLVQH 203
Cdd:cd04409   177 GPTLIRPrPTDATVSL---SSLVDY 198

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  45 QCVDFIRERGLSEEGLFRMPGQ----ANLVRDLQDSFDCGeKPlFDSTTDVHTVASLLKLYLRELPEPVIPFARYEDFLS 120
Cdd:cd04380    56 RLVDYLYTRGLAQEGLFEEPGLpsepGELLAEIRDALDTG-SP-FNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907101034 121 CAQLltkdegegTVELAKQV--SNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNLATVFGPNILRPQIEDP 191
Cdd:cd04380   134 AVAN--------NEEDKRQVirISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAG 198

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  20 FGQRLEDTVHHERKF-GPRLaPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTtDVHTVASLL 98
Cdd:cd04381     1 FGASLSLAVERSRCHdGIDL-PLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEY-EPPTVASLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101034  99 KLYLRELPEPVIP---FARYEDflSCAqllTKDEGEGTVELAKQVSNLPQANYNLLRYICKFLDEVQAHSDVNKMSVQNL 175
Cdd:cd04381    79 KQYLRELPEPLLTkelMPRFEE--ACG---RPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNI 153

                  ....*...
gi 1907101034 176 ATVFGPNI 183
Cdd:cd04381   154 SIVLSPTV 161