6Q83,1KPS,3RCZ,4JUE,4L83,6GUM


Conserved Protein Domain Family
UBCc_UBE2I

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cd23798: UBCc_UBE2I 
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I and related proteins
The E2I subfamily includes mammalian ubiquitin-conjugating enzymes E2 I (UBE2I/UBC9/UBCE9, EC 2.3.2.-), yeast ubiquitin-conjugating enzyme E2-18 kDa (UBC9, EC2.3.2.-), and plant SUMO-conjugating enzyme 1 (SCE1/AHUS5, EC2.3.2.-). UBE2I, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, SUMO-protein ligase, ubiquitin carrier protein 9, ubiquitin carrier protein I, or ubiquitin-protein ligase I, accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. It can catalyze the formation of poly-SUMO chains. It is necessary for sumoylation of FOXL2 and KAT5 and essential for nuclear architecture and chromosome segregation. UBE2I also sumoylates p53/TP53 at 'Lys-386' and mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity. Saccharomyces cerevisiae UBC9, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, ubiquitin carrier protein 9, ubiquitin-conjugating enzyme E2-18 kDa, acts as an E2 ubiquitin-like--protein ligase that mediates SUMO/Smt3 attachment to septins and PCNA. It may be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2). Arabidopsis thaliana SCE1, also called SUMO-conjugating enzyme SCE1, protein EMBRYO DEFECTIVE 1637, or protein hus5 homolog, is a SUMO-conjugating enzyme that accepts the SUMO proteins from the E1 SUMO-activating heterodimer SAE1/SAE2 and catalyzes its covalent attachment to other proteins with the E3 SUMO ligases SIZ1 and MMS21. It associates with SIZ1 for sumoylation of the transcription factor GTE3.
Statistics
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PSSM-Id: 467418
Aligned: 80 rows
Threshold Bit Score: 191.981
Created: 10-Aug-2017
Updated: 27-Apr-2023
Structure
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Program:
Drawing:
Aligned Rows:
 
active site
Conserved site include 1 residue -Click on image for an interactive view with Cn3D
Feature 1: active site cysteine [active site], 1 residue position
Conserved feature residue pattern:CClick to see conserved feature residue pattern help
Evidence:
  • Comment:forms a thioester with ubiquitin or ubiquitin-like proteins
  • Comment:serves as the point of attachment of ubiquitin prior to transfer to cellular target
  • Citation:PMID 9497353
  • Citation:PMID 9705497

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                        
6Q83_B         4 LCLQRLQEERKKWRKDHPFGFYAKPVKkaDGSMDLQKWEAGIPGKegtNWAGGVYPITVEYPneYPSKPPKVKFPaGFYH 83  Saccharomyces c...
EDV28851       8 DPVERLQAEHRIWKISHPKDFEADPMIasDGSEDWLTWLCVIPGPtktCWENGRFRLMIYYPkdYPDKPPKCQFQpPLFH 87  Trichoplax adha...
KRZ72435      37 EVARRVCEQFVAYKKKYGFNFIAKPVTk-NGQEDFSEWICGFPGRkgtLWEGALLKLRVTFPsnYPVEPPAFIFDpPIPH 115 Trichinella papuae
KXJ14594       9 DPVERLKEEHKAWKCFHPKDFIANPLKreDGTINWLVWKCAIPGPxktPWEGGLFPLRLEFPqdYPFSPPKCIFTpSILH 88  Exaiptasia pallida
ORX59049       4 LCISRLIEERNQLKKDFIPGFKAGPLKtkDGNYDILNWEAYIPGIrgtSWDGGIFKLNLKFSkdYPLKPPKCTFNpPVFH 83  Anaeromyces sp....
KAI3640460     3 ITQVRLQEERKLWRKDHPFGFSAKPRKnaDGTLNLMIWDCGIPGPkgsLWEGGTYMLTLTFPatYPAAPPKCQFNpVILH 82  Amoeboaphelidiu...
KAI3633959     5 MAVMRLTEERKLWKKDHPFGFIAKPMKksDGTLDLMNWHCAVPGVkgtLWEGGLYTVKLHFNanYPSEPPKCVFSpPIYH 84  Amoeboaphelidiu...
XP_012557628   8 IADERLKEEYNAWKVNHPLDFKAEPLKn-GDIENWKIWNCSVPGVektSWEGGNYKLRLEFTdqYPHEPPKCIFDpPIFH 86  Hydra vulgaris
KRZ36625       4 ESLRKLIEDHRSWNENHPAGFFANPLRv-GEKYDFYNWVCYIPGAkesSWEGGLYQLLMWFPenYPYTPPRCTFIpPLFH 82  Trichinella pse...
NP_498198     35 NEINTVKEEKAKWDERTPQGYTAKPISf-EGADIWCSWICTVPGPrgsPWEGGEYEVSVNFHk-WPIIPPICEFKtPLHH 112 Caenorhabditis ...
Feature 1                 #                                                                      
6Q83_B        84 PNVYPSGTICLSILned--------------------------qdWRPAITLKQIVLGVQDLLDSPNp--------NSPA 129 Saccharomyces c...
EDV28851      88 PNIFLSGTVALSILeedwkptltikdvmpkicheifnykscalfcNSPSSIIEVILPGIQMLLKEPNm--------NNPA 159 Trichoplax adha...
KRZ72435     116 PNVYPNGYVCLSMLdq---------------------------tnWKQGTTVSQLFKALDNIMDHPDr--------ENPA 160 Trichinella papuae
KXJ14594      89 PNVFPSGTVCLSLIdkn--------------------------kdWKPQVTMKQVLQGIQLLLQDPNf--------LEPA 134 Exaiptasia pallida
ORX59049      84 PNIYLSGDVCLSILney--------------------------edWKPSISIRDILIGIQLLLNEPNl--------ESPA 129 Anaeromyces sp....
KAI3640460    83 PNIFPSGTVCLSITnpd--------------------------kgWKPSITIKQILLGIQQLLHEVNn--------DDPA 128 Amoeboaphelidiu...
KAI3633959    85 PNVWESGMICLSIIdpr--------------------------sgWRPSITIKQILLGIQQLLDEVRlqeerklwrKDHP 138 Amoeboaphelidiu...
XP_012557628  87 PNVFPSGKVSLSLLek----------------------------dWVPQITIKQVLLGIQLLLNDPNf--------NDPA 130 Hydra vulgaris
KRZ36625      83 PNIHASGVVQWSFLdss--------------------------kqWIPSMKIGDILIGLQQLLAEPCl--------DEVV 128 Trichinella pse...
NP_498198    113 PNVDLRGSIYLKMLeq---------------------------ehWSSETSLKKLLREISNLLATPDl--------TQAA 157 Caenorhabditis ...
Feature 1                                       
6Q83_B       130 QEPAWRSFSRn-----KAEYDKKVLLQAKQY 155 Saccharomyces cerevisiae S288C
EDV28851     160 HAMAYTLHKTs-----LFEYNNRIRQQVAKS 185 Trichoplax adhaerens
KRZ72435     161 NAVAFFEFCEr-----PEKYNERMRKAAKKF 186 Trichinella papuae
KXJ14594     135 QAEAFMIHSQs-----SLDYENKVKAFAKQM 160 Exaiptasia pallida
ORX59049     130 QHAAYALYQEn-----RLEYEKRLMIQSKNH 155 Anaeromyces sp. KS-2015
KAI3640460   129 NGEVSMIYRQn-----RPKYEQMVRDQAKKY 154 Amoeboaphelidium protococcarum
KAI3633959   139 FGFSAKPRKNadgtlnLMIWDCGIPGPKGSL 169 Amoeboaphelidium protococcarum
XP_012557628 131 QVEAFVVHSKg-----KHLYEQRVKEQAKLM 156 Hydra vulgaris
KRZ36625     129 HNEAYTVLCTd-----PAAYDFIIQHLAKKF 154 Trichinella pseudospiralis
NP_498198    158 NIEAWMEYENq-----RENYEAKARAYAWTV 183 Caenorhabditis elegans

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