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Conserved domains on  [gi|251757431|sp|Q8N2K1|]
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RecName: Full=Ubiquitin-conjugating enzyme E2 J2; AltName: Full=Non-canonical ubiquitin-conjugating enzyme 2; Short=NCUBE-2 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
UBCc cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain. This is part of the ...
14-127 3.22e-47

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain. This is part of the ubiquitin-mediated protein degradation pathway in which a thiol-ester linkage forms between a conserved cysteine and the C-terminus of ubiquitin and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thiol-ester linkages without the use of E3s as well as several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) which lack the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways which were omitted from the scope of this CD.


:

Pssm-ID: 238117  Cd Length: 141  Bit Score: 155.82  E-value: 3.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  14 TQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMIT--PNGRFKCNT 91
Cdd:cd00195    1 SKRLQKELKDLKKDPPSGISAEPVEENLLEWHGTIRGPPDTPYEGGIFKLDIEFPEDYPFKPPKVRFVTkiYHPNVDENG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 251757431  92 RLCLSITDFHpdTWNPAWSVSTILTGLLSFMVEKGP 127
Cdd:cd00195   81 KICLSILKTH--GWSPAYTLRTVLLSLQSLLNEPNP 114
 
Name Accession Description Interval E-value
UBCc cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain. This is part of the ...
14-127 3.22e-47

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain. This is part of the ubiquitin-mediated protein degradation pathway in which a thiol-ester linkage forms between a conserved cysteine and the C-terminus of ubiquitin and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thiol-ester linkages without the use of E3s as well as several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) which lack the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways which were omitted from the scope of this CD.


Pssm-ID: 238117  Cd Length: 141  Bit Score: 155.82  E-value: 3.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  14 TQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMIT--PNGRFKCNT 91
Cdd:cd00195    1 SKRLQKELKDLKKDPPSGISAEPVEENLLEWHGTIRGPPDTPYEGGIFKLDIEFPEDYPFKPPKVRFVTkiYHPNVDENG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 251757431  92 RLCLSITDFHpdTWNPAWSVSTILTGLLSFMVEKGP 127
Cdd:cd00195   81 KICLSILKTH--GWSPAYTLRTVLLSLQSLLNEPNP 114
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
16-128 1.38e-37

Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 249657  Cd Length: 139  Bit Score: 130.41  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431   16 RLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMITPngRFKCNT---- 91
Cdd:pfam00179   1 RLQKELKLLQKDPPPGISAFPVDDNLFEWEVTIIGPEGTPYEGGVFKLSIEFPEDYPFKPPKVKFTTK--IYHPNVdpsg 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 251757431   92 RLCLSItdFHPDTWNPAWSVSTILTGLLSFMVEKGPT 128
Cdd:pfam00179  79 EVCLDI--LKDENWSPALTVEQVLLSIQSLLSEPNPE 113
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]
12-124 2.79e-36

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 227410  Cd Length: 153  Bit Score: 127.76  E-value: 2.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  12 TATQRLKQDYLRIKKDPVPYICAEPL-PSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMITPNGRFKCN 90
Cdd:COG5078    5 SALKRLLKELKKLQKDPPPGISAGPVdDDNLFHWEATITGPPDTPYEGGIFKLTLEFPEDYPFKPPKVRFTTKIFHPNVD 84
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 251757431  91 T--RLCLSITDfhpDTWNPAWSVSTILTGLLSFMVE 124
Cdd:COG5078   85 PsgNVCLDILK---DRWSPVYTLETILLSLQSLLLS 117
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
16-124 1.74e-33

Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. This pathway functions in regulating many fundamental processes required for cell viability.TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 214562  Cd Length: 145  Bit Score: 120.09  E-value: 1.74e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431    16 RLKQDYLRIKKDPVPYICAEPLP-SNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMITP--NGRFKCNTR 92
Cdd:smart00212   1 RLLKELKELRKDPPPGFTAYPVDdENLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKPPKVKFITKiyHPNVDSSGE 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 251757431    93 LCLSItdFHPDTWNPAWSVSTILTGLLSFMVE 124
Cdd:smart00212  81 ICLDI--LKQEKWSPALTLETVLLSLQSLLSE 110
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
13-127 2.66e-18

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768  Cd Length: 147  Bit Score: 78.64  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  13 ATQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMIT----PNgrFK 88
Cdd:PLN00172   2 ATKRIQKEHKDLLKDPPSNCSAGPSDENLFRWTASIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTTkiyhPN--IN 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 251757431  89 CNTRLCLSITDfhpDTWNPAWSVSTILTGLLSFMVEKGP 127
Cdd:PLN00172  80 SNGSICLDILR---DQWSPALTVSKVLLSISSLLTDPNP 115
PTZ00390 PTZ00390
ubiquitin-conjugating enzyme; Provisional
12-115 1.35e-16

ubiquitin-conjugating enzyme; Provisional


Pssm-ID: 240397  Cd Length: 152  Bit Score: 73.69  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  12 TATQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMIT----PNgrF 87
Cdd:PTZ00390   2 SISKRIEKETQNLANDPPPGIKAEPDPGNYRHFKILMEGPDGTPYEGGYYKLELFLPEQYPMEPPKVRFLTkiyhPN--I 79
                         90       100
                 ....*....|....*....|....*...
gi 251757431  88 KCNTRLCLSITDfhpDTWNPAWSVSTIL 115
Cdd:PTZ00390  80 DKLGRICLDILK---DKWSPALQIRTVL 104
 
Name Accession Description Interval E-value
UBCc cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain. This is part of the ...
14-127 3.22e-47

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain. This is part of the ubiquitin-mediated protein degradation pathway in which a thiol-ester linkage forms between a conserved cysteine and the C-terminus of ubiquitin and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thiol-ester linkages without the use of E3s as well as several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) which lack the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways which were omitted from the scope of this CD.


Pssm-ID: 238117  Cd Length: 141  Bit Score: 155.82  E-value: 3.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  14 TQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMIT--PNGRFKCNT 91
Cdd:cd00195    1 SKRLQKELKDLKKDPPSGISAEPVEENLLEWHGTIRGPPDTPYEGGIFKLDIEFPEDYPFKPPKVRFVTkiYHPNVDENG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 251757431  92 RLCLSITDFHpdTWNPAWSVSTILTGLLSFMVEKGP 127
Cdd:cd00195   81 KICLSILKTH--GWSPAYTLRTVLLSLQSLLNEPNP 114
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
16-128 1.38e-37

Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 249657  Cd Length: 139  Bit Score: 130.41  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431   16 RLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMITPngRFKCNT---- 91
Cdd:pfam00179   1 RLQKELKLLQKDPPPGISAFPVDDNLFEWEVTIIGPEGTPYEGGVFKLSIEFPEDYPFKPPKVKFTTK--IYHPNVdpsg 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 251757431   92 RLCLSItdFHPDTWNPAWSVSTILTGLLSFMVEKGPT 128
Cdd:pfam00179  79 EVCLDI--LKDENWSPALTVEQVLLSIQSLLSEPNPE 113
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]
12-124 2.79e-36

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 227410  Cd Length: 153  Bit Score: 127.76  E-value: 2.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  12 TATQRLKQDYLRIKKDPVPYICAEPL-PSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMITPNGRFKCN 90
Cdd:COG5078    5 SALKRLLKELKKLQKDPPPGISAGPVdDDNLFHWEATITGPPDTPYEGGIFKLTLEFPEDYPFKPPKVRFTTKIFHPNVD 84
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 251757431  91 T--RLCLSITDfhpDTWNPAWSVSTILTGLLSFMVE 124
Cdd:COG5078   85 PsgNVCLDILK---DRWSPVYTLETILLSLQSLLLS 117
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
16-124 1.74e-33

Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. This pathway functions in regulating many fundamental processes required for cell viability.TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 214562  Cd Length: 145  Bit Score: 120.09  E-value: 1.74e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431    16 RLKQDYLRIKKDPVPYICAEPLP-SNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMITP--NGRFKCNTR 92
Cdd:smart00212   1 RLLKELKELRKDPPPGFTAYPVDdENLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKPPKVKFITKiyHPNVDSSGE 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 251757431    93 LCLSItdFHPDTWNPAWSVSTILTGLLSFMVE 124
Cdd:smart00212  81 ICLDI--LKQEKWSPALTLETVLLSLQSLLSE 110
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
13-127 2.66e-18

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768  Cd Length: 147  Bit Score: 78.64  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  13 ATQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMIT----PNgrFK 88
Cdd:PLN00172   2 ATKRIQKEHKDLLKDPPSNCSAGPSDENLFRWTASIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTTkiyhPN--IN 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 251757431  89 CNTRLCLSITDfhpDTWNPAWSVSTILTGLLSFMVEKGP 127
Cdd:PLN00172  80 SNGSICLDILR---DQWSPALTVSKVLLSISSLLTDPNP 115
PTZ00390 PTZ00390
ubiquitin-conjugating enzyme; Provisional
12-115 1.35e-16

ubiquitin-conjugating enzyme; Provisional


Pssm-ID: 240397  Cd Length: 152  Bit Score: 73.69  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251757431  12 TATQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMIT----PNgrF 87
Cdd:PTZ00390   2 SISKRIEKETQNLANDPPPGIKAEPDPGNYRHFKILMEGPDGTPYEGGYYKLELFLPEQYPMEPPKVRFLTkiyhPN--I 79
                         90       100
                 ....*....|....*....|....*...
gi 251757431  88 KCNTRLCLSITDfhpDTWNPAWSVSTIL 115
Cdd:PTZ00390  80 DKLGRICLDILK---DKWSPALQIRTVL 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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