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cd00196: UBQ 
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Ubiquitin homologs; Includes ubiquitin and ubiquitin-like proteins. Ubiquitin-mediated proteolysis is part of the regulated turnover of proteins required for controlling cell cycle progression. Other family members are protein modifiers that perform a wide range of functions. Ubiquitination usually results in a covalent bond between the c-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. The three-step mechanism requires an activating enzyme (E1) that forms a thiol ester with the c-terminal carboxy group, a conjugating enzyme (E2) that transiently carries the activated ubiquitin molecule as a thiol ester, and a ligase (E3) that transfers the activated ubiquitin from the E2 to the substrate lysine residue. In poly-ubiquitination ubiquitin itself is the substrate.
Statistics
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PSSM-Id: 5394
View PSSM: cd00196
Aligned: 53 rows
Threshold Bit Score: -1
Threshold Setting Gi: 0
Created: 1-Nov-2000
Updated: 17-Apr-2002
Structure
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Program:
Drawing:
Aligned Rows:
 
hydrophobiccharged pocket
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:hydrophobic patch
Evidence:
  • Comment:surface patch shown to be essential for proteolytic targeting in some ubiquitins
  • Citation:PMID 9857029
  • Citation:PMID 8570649
  • Structure:Ubal (1CMX_B) interacts with yUH1 (1CMX_A)
    View structure with Cn3D
  • Structure:Ulp1 Protease (1EUV_B) interacts with Smt3 (1EUV_A)
    View structure with Cn3D

This CD has no sequence tree.
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                      ####                            
1CMX_B       1 MQIFVKTlt--gKTITLEVEPS-DTIENVKAKIQDke--gIPPDQQRLIFAGKQL-----EDGRt-lSDYNIQk-eSTLH 68
gi 465686  343 ILIKLKFm---nDTEKNTYASLeDTVAKFKVDHFTn----LANQVIRLIYQGQLL-----REDHrtlEEYGLQp-gSIVH 409
gi 1174863   6 FEFNIRHs---gKVYPITLSTD-ATSADLKSKAEElt--qVPSARQKYMVKGGLS-----GEESi--KIYPLIkpgSTVM 72
gi 1747519 258 FTLKIRCr---aDLVRLPVRMS-EPLQNVVDHMANhl--gVSPNRILLLFGESEL-----SPTAt-pSTLKLGv-aDIID 324
gi 1944138 348 VKVQVKQlq--gMSLTRKVHPS-TTVWELKGEIEKew--cIPRYQQRLALQDNPSnlpalRDGDs-lAAHGLFy-dIVLL 420
gi 2501445  18 INLKVAGqd--gSVVQFKIKRH-TPLSKLMKAYCErq--gLSMRQIRFRFDGQPI-----NETDt-pAQLEMEd-eDTID 85
gi 2501461   2 PIVNVKWq---kEKYVVEVDTS-APPMVFKAQLFAlt--qVVPERQKVVIMGRTL-----GDDDw--EGITIKe-nMTIM 67
gi 5454144   8 LCVHVRSee--wDLMTFDANPY-DSVKKIKEHVRSk---tKVPVQDQVLLLGSKIl----KPRRs-lSSYGIDk-eKTIH 75
gi 6324461  74 VHLTLKKiqapkFSIEHDFSPS-DTILQIKQHLISee-kaSHISEIKLLLKGKVL-----HDNLf-lSDLKVTp-aNSTI 144
gi 7511023  52 LSVTFRTlt--qVNFNLELNED-QTIAEVKALVASekgddYAPELQKLIYNGKIL-----DDSVk-vGEVGFDs-sKFVV 121

               ....
Feature 1       ## 
1CMX_B      69 LVLR 72
gi 465686  410 CHIS 413
gi 1174863  73 LLGT 76
gi 1747519 325 CVVL 328
gi 1944138 421 LLCT 424
gi 2501445  86 VFQQ 89
gi 2501461  68 MMGS 71
gi 5454144  76 LTLK 79
gi 6324461 145 TVMI 148
gi 7511023 122 VMLS 125

Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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Conserved site includes 6 residues -Click on image for an interactive view with Cn3D