2EW1


Conserved Protein Domain Family
Rab30

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cd04114: Rab30 
Click on image for an interactive view with Cn3D
Rab GTPase family 30 (Rab30)
Rab30 subfamily. Rab30 appears to be associated with the Golgi stack. It is expressed in a wide variety of tissue types and in humans maps to chromosome 11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab 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: 133314
View PSSM: cd04114
Aligned: 6 rows
Threshold Bit Score: 338.41
Threshold Setting Gi: 17555898
Created: 9-Aug-2005
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 16 residues -Click on image for an interactive view with Cn3D
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Comment:The active conformation of Rab is stabilized by interations between the gamma phosphate of GTP and two critically conserved residues, Thr in switch I and Gly in switch II
  • Structure:2EWI: Human Rab30 binds GppNHp, a GTP analog and Mg2+, defined using 3.5 A contacts
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                      #######         #     ##                         #               
2EW1_A       20 MEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSA 99
gi 38258937   3 MEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSA 82
gi 57526504   1 MEDYDYLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEIKGVKVKLQIWDTAGQERFRSITQSYYRSA 80
gi 17555898   1 MEDYKYLFKVVLVGNAGVGKTCLVRKFTQGIFPPGQSATIGVDFMIKTVKVGNDKIKLQIWDTAGQERFRSITQSYYRSA 80
gi 47937791   3 MEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEIKGEKIKLQIWDTAGQERFRSITQSYYRSA 82
gi 24582410   1 MEDYKFLFKIVLVGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEVEGEKIKLQIWDTAGQERFRSITQSYYRSA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                              ## #                            ##       
2EW1_A      100 NALILTYDITCEESFRCLPEWLREIEQYASNKVITVLVGNKIDLaerREVSQQRAEEFSEAQd-mYYLETSAKESDNVEK 178
gi 38258937  83 NALILTYDITCEESFRCLPEWLREIEQYASNKVITVLVGNKIDLaerREVSQQRAEEFSEAQd-mYYLETSAKESDNVEK 161
gi 57526504  81 NALILTYDITCEDSFRCLPEWLREIEQYANNQVVTILVGNKIDLadkREVLRQRAEEFADSQs-mLYLETSAKESDNVEK 159
gi 17555898  81 HAIVLVYDVSCQPSFDCLPEWLGEIESYANRRVLKILVGNKVDKgdeREVPERIGRDFSDVNqfdYFLETSALDATNVDQ 160
gi 47937791  83 NALILTYDITCEESFRCLPEWLREIEQYASSEVITVLVGNKIDLaerREVSQQRAEEFAGTQn-mYYLETSAKESDNVEK 161
gi 24582410  81 HALILVYDISCQPTFDCLPDWLREIQEYANSKVLKILVGNKTDRd-dREIPTQIGEEFAKQHd-mYFLETSAKEAENVER 158
                       170
                ....*....|
Feature 1                 
2EW1_A      179 LFLDLACRLI 188
gi 38258937 162 LFLDLACRLI 171
gi 57526504 160 LFLDLACELI 169
gi 17555898 161 LFEQVATRLT 170
gi 47937791 162 LFLDLACRLI 171
gi 24582410 159 LFYEIAAELI 168

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