Conserved Protein Domain Family
Rnd1_Rho6

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cd04174: Rnd1_Rho6 
Rnd1/Rho6 GTPases
Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Statistics
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PSSM-Id: 206737
View PSSM: cd04174
Aligned: 3 rows
Threshold Bit Score: 482.25
Threshold Setting Gi: 5163412
Created: 1-Mar-2006
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 11177004    1 MKERRAPQPVVARCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPL 80
gi 5163412     1 MKERRNPQPAVVRCKLVLVGDVHCGKTAMLQVLAKDCYPETYVPTVFENYTASLETEEQRVELSLWDTSGSPYYDNVRPL 80
gi 113205049   1 MKERRNAQPLVVRCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLELDDQRVELSLWDTSGSPYYDNVRPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                     # #                                
gi 11177004   81 CYSDSDAVLLCFDISRPETVDSALKKWRTEILDYCPSTRVLLIGCKTDLRTDLSTLMELSHQKQAPISYEQGCAIAKQLG 160
gi 5163412    81 CYSDSDAVLLCFDISRPESLDSAMKKWKSEITDYCPNTRILLIGCKTDLRTDLSTIMELSNQKQAPVSYEQGCAVAKQLG 160
gi 113205049  81 CYSDSDAVLLCFDISRPDIFDSGLKKWRAEILDFCPSTRILLVGCKTDLRTDVCTLMELSNQKQTPITHEQGSAMAKQLG 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
Feature 1                ##                                                              
gi 11177004  161 AEIYLEGSAFTSEKSIHSIFRTASMLCLNKPSPLPQKSPVRSLSKRLLHLPSRSELISSTFKKEKAKSCSIM 232
gi 5163412   161 AENYLECSAFTSEKSVHSIFRAASSLCVNKASPASRKSPVRSLSKRLLNLPSRSEIISSTFKKEKAKSCCLM 232
gi 113205049 161 AEAYLECSAFTSEKSIHSVFRTAALACINKLQPLAKPSPTRRLSKRLLHLPSKSELLSSTFKKEKAKSCSVM 232

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