Conserved Protein Domain Family
Rho2

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cd04129: Rho2 
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases)
Rho2 is a fungal GTPase that plays a role in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Rho2 activates the protein kinase C homolog Pck2, and Pck2 controls Mok1, the major (1-3) alpha-D-glucan synthase. Together with Rho1 (RhoA), Rho2 regulates the construction of the cell wall. Unlike Rho1, Rho2 is not an essential protein, but its overexpression is lethal. 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 proper intracellular localization via membrane attachment. As with other Rho family GTPases, the GDP/GTP cycling is regulated by GEFs (guanine nucleotide exchange factors), GAPs (GTPase-activating proteins) and GDIs (guanine nucleotide dissociation inhibitors).
Statistics
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PSSM-Id: 206702
Aligned: 5 rows
Threshold Bit Score: 351.828
Created: 3-Jan-2006
Updated: 2-Oct-2020
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:
Feature 1               ######                                      ## #                      
CAB57399    8 RRKLVVVGDGACGKTSLLSVFTLGYFPTEYVPTVFENYVSDCRVDGKSVQLALWDTAGQEEYERLRPMSYAKAHIILVGF 87  fission yeast
AAW44403   11 RRKLVIVGDGAAGKTSLLNVFAVGHFSESYEPTVFDNYVTEIELDGKPVQLALWDTAGQEEYERLRPLSYSKAHVILIAF 90  Cryptococcus neofo...
XP_758641   7 RRKLVIVGDGACGKTSLLCVFAIGEFPQEYEPTIFENYVAEIRLDGKPVQLALWDTAGQEEYERLRPLSYSQAHVILIAF 86  Ustilago maydis 521
CAG86098    7 KRKIVIVGDGACGKTSLLFVFTLGEFPTEYHPTVFENYVTDCRVDGKAVQLALWDTAGQEEYERLRPLSYANSHVILIGF 86  Debaryomyces hanse...
CAA95965    7 RRKLVIIGDGACGKTSLLYVFTLGKFPEQYHPTVFENYVTDCRVDGIKVSLTLWDTAGQEEYERLRPFSYSKADIILIGF 86  baker's yeast
Feature 1                                       # #                                        ## 
CAB57399   88 AIDSPDSLENVSTKWIEEINTLCpn-vPFILVGMKADLRsdpvaieemrrrnqnfvkSQQAELVAQRIGARKYMECSSLT 166 fission yeast
AAW44403   91 AVDTPDSLENVTQKWIEEVRSICgkaiPVILVACKADLRdkavangt--ysperftdHATGQRIADSIGAKGYFETSALQ 168 Cryptococcus neofo...
XP_758641  87 AIDTPDSLENVQVKWMEEVRQICgpsvPVLLVGCKKDLRedaiakgk--pvqghyveRQQAKLVAAQIGARSYHECSSLN 164 Ustilago maydis 521
CAG86098   87 AIDVPDSLDNARTKWVEEVTKYCpn-tPYLLIGLKKDLRvessnr-------rkyvqFHQGEIAAKEMHAKKYLESSALY 158 Debaryomyces hanse...
CAA95965   87 AVDNFESLINARTKWADEALRYCpd-aPIVLVGLKKDLRqeahfken---atdemvpIEDAKQVARAIGAKKYMECSALT 162 baker's yeast
Feature 1                                                            
CAB57399  167 GDGVDDVFEAATRAAltvrdse----------------------ndksstkCCII 199 fission yeast
AAW44403  169 NRNVDAVFEAATRAAvlvrdaghggvgapngsfdaggrkdwgrekeekkfgCCVI 223 Cryptococcus neoformans var. neoformans JEC21
XP_758641 165 NQGVDAVFEAATRAAmlvrnsgassggais-------qsktkealhndagsCKCI 212 Ustilago maydis 521
CAG86098  159 GEGVDDIFEYATRTSllvqk---------------------------anqtCCTI 186 Debaryomyces hansenii CBS767
CAA95965  163 GEGVDDVFEVATRTSllmkk--------------------------epganCCII 191 baker's yeast

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