Conserved Protein Domain Family
Rho3

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cd04134: Rho3 
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases)
Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.
Statistics
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PSSM-Id: 206706
View PSSM: cd04134
Aligned: 4 rows
Threshold Bit Score: 327.587
Threshold Setting Gi: 71019973
Created: 30-Dec-2005
Updated: 17-Jan-2013
Structure
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Aligned Rows:
  next features
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Comment:Rho molecules assume an active conformation when bound to GTP and inactive when GTP is hydrolyzed to GDP
  • Comment:Mg2+ ion plays a key role in bringing together the functional regions of the phosphate-binding, switches I and II
  • Citation:PMID 9545299

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                ######                                       ## #                      
gi 29420023  14 RKIVILGDGAAGKTSLLNVFTKGYFPQVYEPTIFENYIHDIFvd-gnSIELSLWDTAGQEEYDQLRSLSYsDTHVIMICF 92
gi 12230529  18 RKVVVCGDGACGKTSLLNVFTRGFFTQVYEPTVFENYVHDLYid-dqLVELSLWDTAGQEEFDRLRSLSYaETHVIMICF 96
gi 71019973  19 RKVLVLGDGASGKTSLLFVLVRHEFPQTYEPTVFENYTHIQHthtglAVELTLWDTAGQEEFDKLRSLSYaDTDVVLLCF 98
gi 599999    17 RKIVILGDGACGKTSLLNVFTRGYFPEVYEPTVFENYIHDIFvd-skHITLSLWDTAGQEEFDRLRSLSYsDTQCIMLCF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                        # #                                            
gi 29420023  93 AVDSRDSLENVITKWLPEVSSNCPGVKLVLVALKCDLRGadeeqvd-------------------------hskiidyEE 147
gi 12230529  97 SVDNPTSLENVESKWLDEILEYCPGVKLVLVDSKCDLRDdpavldrlq---------------------rygthtdqyEE 155
gi 71019973  99 SVDNPVSLQNVESRWIAEIRHHCPAVKIMLVALKCDLREprnpr------------------------------tlsyNH 148
gi 599999    96 SIDSRDSLENVQNKWVGEITDHCEGVKLVLVALKCDLRNnenesnaitpnniqqdnsvsndngnninstsngknlisyEE 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
Feature 1                        ##                                       
gi 29420023 148 GLAAAKKINAvRYLECSAKLNrGVNEAFTEAARValaaqprgtkdgadeshgTGCIIA 205
gi 12230529 156 GLGVARRIRAsRYLECSSKHNrGVNEVFLRGRARvtvhsi-------rqgsaGSCCVM 206
gi 71019973 149 GLDVAKRINAcRYLECSAKSNrGVTECFTELASVaanvr--------phphsRACTIA 198
gi 599999   176 GLAMAKKIGAlRYLECSAKLNkGVNEAFTEAARValtagp------vatevkSDSGSS 227

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