3KYD,3KYC,1A5R,1TGZ,1Y8R,1Z5S,2BF8,2G4D,2IY0,2IY1,2KQS,2LAS,2UYZ,3RZW,4WJN,5AEK,5ELJ


Conserved Protein Domain Family
Ubl_SUMO1

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cd16114: Ubl_SUMO1 
Click on image for an interactive view with Cn3D
ubiquitin-like (Ubl) domain found in small ubiquitin-related modifier 1 (SUMO-1) and similar proteins
SUMO (also known as "Smt3" and "sentrin" in other organisms) resembles ubiquitin (Ub) in structure, ligation to other proteins and the mechanism of ligation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. SUMOs, like Ub, are covalently conjugated to lysine residues in a wide variety of target proteins in eukaryotic cells and regulate numerous cellular processes, such as transcription, epigenetic gene control, genomic instability, and protein degradation. Four SUMO paralogs exist in mammals, SUMO1 through SUMO4. SUMO2-SUMO4 are more closely related to each other than they are to SUMO1. SUMO1 is a binding partner of the RAD51/52 nucleoprotein filament proteins, which mediate DNA strand exchange. SUMO1 conjugation to cellular proteins has been implicated in multiple important cellular processes, such as nuclear transport, cell cycle control, oncogenesis, inflammation, and the response to virus infection.
Statistics
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PSSM-Id: 340531
Aligned: 32 rows
Threshold Bit Score: 125.647
Created: 3-Mar-2015
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 18 residues -Click on image for an interactive view with Cn3D
Feature 1:SUMO1-SAE2-SAE1-ATP-Mg complex [polypeptide binding site]
Evidence:
  • Comment:Heterodimer of SAE1 (SUMO-activating enzyme E1) and SAE2 in mammals activates SUMO proteins in an ATP-dependent manner.
  • Structure:1Y8R; Homo sapiens SUMO1 in complex with SAE1-SAE2-ATP-Mg, contacts at 4A.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                ###                          # ## #   ####                  # ######
3KYD_D        40 YIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQCG 115 human
1Y8R_C        21 YIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTG 96  human
P55853        14 YIKIKVVGQDSNEVHFRVKYGTSMAKLKKSYADRTGVAVNSLRFLFDGRRINDDDTPKTLEMEDDDVIEVYQEQLG 89  nematode
XP_002411230  18 YIKLKVVGQDGNEIHFKVKMTTQMGKLKKSYSERVAMSVASLRFLFDGKRINDDETPKQLEMVNDDVIEVYQEQTG 93  black-legged tick
XP_002594040  21 YIKLKVMGQDNSEIHFKVKMTTQMRKLKESYCQRQGVPINSLRFLFDGQRINDDQTPKELEMTDNDIIEVYQEQTG 96  Florida lancelet
EFX73744      16 YIKLKVVGQDSNEIHFRVKMTTQMGKLKKSYSERVGVPVTSLRFLFDGRRINDDETPKQLEMENDDVIEVYQEQTG 91  common water flea
EGI67360     114 YIKLKVVGNDSNEIHFRVKMTTQMGKLKKSYSDRVGVPMTSLRFLFDGKRINDDETPKQLEMENDDVIEVYQEQTG 189 Panamanian leafcutt...
XP_006821439  26 YIKLKVMGQDNSEIHFKVKMTTQMRKLKESYCQRLGVPMNSLRFLFDGQRINDDMTPKELEMETDDVIEVYQEQTG 101 Saccoglossus kowale...
XP_007888824  31 YIKLKVIGQDNSEIHFKVKMTTQLKKLKESYCQRQGVPMNSLRFLFEGQRIGDHQTPKELGMEDEDVIEVYQEQTG 106 elephant shark
XP_013388698  29 YIKLKVVGQDGSEIHFKVKMNTQMGRLKKSYSDRQGIPLNSLRFLFDGRRINDDETPKQLEMDDSDCIEVYQEQTG 104 Lingula anatina

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