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Conserved domains on  [gi|19527004|ref|NP_598538|]
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ubiquitin-conjugating enzyme E2 S [Mus musculus]

Protein Classification

ubiquitin-conjugating enzyme family protein( domain architecture ID 10445965)

ubiquitin-conjugating enzyme family protein similar to ubiquitin-conjugating enzyme E2 that accepts ubiquitin or ubiquitin-like proteins from the E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase

CATH:  3.10.110.10
EC:  2.3.2.-
Gene Ontology:  GO:0004842|GO:0061631|GO:0000209
PubMed:  16732283|19940261|26463729
SCOP:  4001046

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBCc_UBE2S cd23804
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S ...
 10-155 9.50e-113

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S and related domains; The E2S subfamily includes mammalian ubiquitin-conjugating enzymes E2 S (UBE2S/E2EPF), plant ubiquitin-conjugating enzyme E2 22 (UBC22), and similar proteins. They are ubiquitin-conjugating enzymes (EC2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2S catalyzes 'Lys-11'-linked polyubiquitination. It acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. It also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro, it can promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination.


:

Pssm-ID: 467424  Cd Length: 146  Bit Score: 318.65  E-value: 9.50e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  10 PHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVG 89
Cdd:cd23804   1 PSVIRRLAKELQSLQSNPPEGIRVIPNEEDLTDIQAEIEGPEGTPYEGGVFRVKLVLGPDFPASPPKGYFLTKIFHPNVS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527004  90 PNGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIH 155
Cdd:cd23804  81 PTGEICVNTLKKDWKPELGLRHILLTIRCLLIEPNPESALNEEAGKLLLEDYDEYAKRARLMTSIH 146
 
Name Accession Description Interval E-value
UBCc_UBE2S cd23804
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S ...
 10-155 9.50e-113

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S and related domains; The E2S subfamily includes mammalian ubiquitin-conjugating enzymes E2 S (UBE2S/E2EPF), plant ubiquitin-conjugating enzyme E2 22 (UBC22), and similar proteins. They are ubiquitin-conjugating enzymes (EC2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2S catalyzes 'Lys-11'-linked polyubiquitination. It acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. It also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro, it can promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination.


Pssm-ID: 467424  Cd Length: 146  Bit Score: 318.65  E-value: 9.50e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  10 PHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVG 89
Cdd:cd23804   1 PSVIRRLAKELQSLQSNPPEGIRVIPNEEDLTDIQAEIEGPEGTPYEGGVFRVKLVLGPDFPASPPKGYFLTKIFHPNVS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527004  90 PNGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIH 155
Cdd:cd23804  81 PTGEICVNTLKKDWKPELGLRHILLTIRCLLIEPNPESALNEEAGKLLLEDYDEYAKRARLMTSIH 146
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 16-152 2.24e-59

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


Pssm-ID: 459701 [Multi-domain]  Cd Length: 139  Bit Score: 183.16  E-value: 2.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004    16 VYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEIC 95
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPDGTPYEGGVFKLSVEFPEDYPFKPPKVKFTTKIYHPNVDSSGEVC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19527004    96 VNVLK-RDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLT 152
Cdd:pfam00179  82 LDILKdERWSPALTLEQVLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVREYV 139
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 18-153 7.81e-50

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 [Multi-domain]  Cd Length: 145  Bit Score: 159.38  E-value: 7.81e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004     18 KEVTTLTADPPDGIKVFP-NEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICV 96
Cdd:smart00212   4 KELKELRKDPPPGFTAYPvDDENLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKPPKVKFITKIYHPNVDSSGEICL 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 19527004     97 NVLK-RDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTE 153
Cdd:smart00212  84 DILKqEKWSPALTLETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTK 141
PTZ00390 PTZ00390
ubiquitin-conjugating enzyme; Provisional
 12-130 3.10e-33

ubiquitin-conjugating enzyme; Provisional


Pssm-ID: 240397  Cd Length: 152  Bit Score: 117.22  E-value: 3.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004   12 IIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN 91
Cdd:PTZ00390   3 ISKRIEKETQNLANDPPPGIKAEPDPGNYRHFKILMEGPDGTPYEGGYYKLELFLPEQYPMEPPKVRFLTKIYHPNIDKL 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19527004   92 GEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALN 130
Cdd:PTZ00390  83 GRICLDILKDKWSPALQIRTVLLSIQALLSAPEPDDPLD 121
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
13-140 3.58e-13

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


Pssm-ID: 444052 [Multi-domain]  Cd Length: 146  Bit Score: 64.35  E-value: 3.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  13 IRLVYKEVTTLTADPPDgIKVFPNEEDLTDLQVTIEGP---EGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNV- 88
Cdd:COG5078  11 LANDYEELENILARGSW-IHFKATRGNPPKYEVTFNIRgiiRGGPTYGDTHRIEITLPESYPQAPPQVRWLTPIFHPNIy 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19527004  89 GPNGEICVNVLKrDWTAELGIRHVLLTIKCLLIHPN--PESALNEEAGRLLLEN 140
Cdd:COG5078  90 EAGGSVCIGRAD-HWTPSLTLDDLIISLARLLQYENyaPHSPVNLEAARWYRSN 142
 
Name Accession Description Interval E-value
UBCc_UBE2S cd23804
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S ...
 10-155 9.50e-113

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S and related domains; The E2S subfamily includes mammalian ubiquitin-conjugating enzymes E2 S (UBE2S/E2EPF), plant ubiquitin-conjugating enzyme E2 22 (UBC22), and similar proteins. They are ubiquitin-conjugating enzymes (EC2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2S catalyzes 'Lys-11'-linked polyubiquitination. It acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. It also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro, it can promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination.


Pssm-ID: 467424  Cd Length: 146  Bit Score: 318.65  E-value: 9.50e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  10 PHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVG 89
Cdd:cd23804   1 PSVIRRLAKELQSLQSNPPEGIRVIPNEEDLTDIQAEIEGPEGTPYEGGVFRVKLVLGPDFPASPPKGYFLTKIFHPNVS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527004  90 PNGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIH 155
Cdd:cd23804  81 PTGEICVNTLKKDWKPELGLRHILLTIRCLLIEPNPESALNEEAGKLLLEDYDEYAKRARLMTSIH 146
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 16-152 2.24e-59

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


Pssm-ID: 459701 [Multi-domain]  Cd Length: 139  Bit Score: 183.16  E-value: 2.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004    16 VYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEIC 95
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPDGTPYEGGVFKLSVEFPEDYPFKPPKVKFTTKIYHPNVDSSGEVC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19527004    96 VNVLK-RDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLT 152
Cdd:pfam00179  82 LDILKdERWSPALTLEQVLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVREYV 139
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 18-153 7.81e-50

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 [Multi-domain]  Cd Length: 145  Bit Score: 159.38  E-value: 7.81e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004     18 KEVTTLTADPPDGIKVFP-NEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICV 96
Cdd:smart00212   4 KELKELRKDPPPGFTAYPvDDENLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKPPKVKFITKIYHPNVDSSGEICL 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 19527004     97 NVLK-RDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTE 153
Cdd:smart00212  84 DILKqEKWSPALTLETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTK 141
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 13-153 5.08e-45

ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; Morgue is an F-box/ubiquitin conjugase domain protein important for grim-reaper mediated apoptosis. It contains both an F-box and a UEV domain that is homologous to E2 ubiquitin ligases but lacks the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467436 [Multi-domain]  Cd Length: 147  Bit Score: 147.00  E-value: 5.08e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  13 IRLVYKEVTTL-TADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN 91
Cdd:cd23826   3 SRRLRRELKALhSDDPPEGISARPLDRSLLHLLATIEGPPGSPYEGGIFFLRIQIPESYPFRPPKVRFLTKIYHPNISRH 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527004  92 GEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTE 153
Cdd:cd23826  83 GDICLDILEHNWSLALTIEKVLISIQSLLTDPYLEDPLVPEIAELYVNDREEFEQTAREWTW 144
UBCc_UBE2N cd23813
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 N ...
 8-155 6.60e-45

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 N and related proteins; The E2N subfamily includes mammalian ubiquitin-conjugating enzymes E2 N (UBE2N/UBCH13/UBC13/BLU), yeast ubiquitin-conjugating enzyme E2 13 (UBC13), and plant ubiquitin-conjugating enzyme E2 35-36 (UBC35/UBC13A/UBG13A, UBC36/UBC13B/UBG13B), which function as ubiquitin-conjugating enzymes (EC 2.3.2.23). UBE2N, also called Bendless-like ubiquitin-conjugating enzyme, forms heterodimers with UBE2V1 and UBE2V2, respectively. The UBE2V1/UBE2N and UBE2V2/UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. UBE2N also plays a role in the control of progress through the cell cycle and differentiation, as well as in the error-free DNA repair pathway, and contributes to the survival of cells after DNA damage. Saccharomyces cerevisiae UBC13 has a role in the DNA error-free post-replication repair (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. Arabidopsis thaliana UBC35 and UBC36 catalyze the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. They mediate transcriptional activation of target genes. They are required for post-replication repair of UV-damaged DNA and for adapting root developmental programs to suboptimal availability of iron.


Pssm-ID: 467433  Cd Length: 144  Bit Score: 146.57  E-value: 6.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004   8 LPPHIIrlvyKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPN 87
Cdd:cd23813   1 LPRRII----KETQRLLAEPVPGISATPDEDNLRYFDVVIDGPPDSPYEGGVFKLELFLPEEYPMAPPKVRFLTKIYHPN 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527004  88 VGPNGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIH 155
Cdd:cd23813  77 IDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEHWKTNEAGAIATAREWTRLY 144
UBCc_UBE2T cd23805
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T ...
 18-155 4.14e-44

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T and related enzymes; The E2T subfamily includes mammalian ubiquitin-conjugating enzymes E2 T (UBE2T/HSPC150/PIG50), plant ubiquitin-conjugating enzyme E2 37 (UBC37), and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2T, also called cell proliferation-inducing gene 50 protein, catalyzes monoubiquitination. It is involved in mitomycin-C (MMC)-induced DNA repair. It acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. UBE2T also mediates monoubiquitination of FANCL and FANCI. It may contribute to ubiquitination and degradation of BRCA1. In vitro, UBE2T can promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.


Pssm-ID: 467425  Cd Length: 146  Bit Score: 144.59  E-value: 4.14e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  18 KEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVN 97
Cdd:cd23805   5 RELQLLQKDPPPGISCWPKDDSLDELEAQIQGPEGTPYEGGVFKLEITIPERYPFEPPKVRFLTPIYHPNIDSAGRICLD 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527004  98 VLKR----DWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIH 155
Cdd:cd23805  85 ILKMppkgSWKPSLNISTVLTSIRLLLAEPNPDDPLMADIAAEYKYNRALFDAKAKEWTKKH 146
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 14-124 6.85e-44

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; The family includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain and ubiquitin (Ub) E2 variant (UEV) domain. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester 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 thioester linkages without the use of E3s. Several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) contains the UEV domain, which lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways.


Pssm-ID: 467407 [Multi-domain]  Cd Length: 112  Bit Score: 142.82  E-value: 6.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGE 93
Cdd:cd00195   1 KRLQKELKELQKNPPPGISVEPVDDDLFHWKATIKGPEGTPYEGGVFKLDIEFPDDYPFKPPKVRFLTPIYHPNVDPDGE 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 19527004  94 ICVNVLKRD-WTAELGIRHVLLTIKCLLIHPN 124
Cdd:cd00195  81 ICLDILKSEgWSPALTLRSVLLSIQSLLSDPN 112
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 14-149 1.04e-38

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 and related proteins; Schizosaccharomyces pombe UBC14 (EC 2.3.2.23), also called ubiquitin-conjugating enzyme E2 14, E2 ubiquitin-conjugating enzyme 14, ubiquitin carrier protein 14, or ubiquitin-protein ligase 14, acts as a ubiquitin-conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. It mediates the selective degradation of short-lived and abnormal proteins.


Pssm-ID: 467435  Cd Length: 143  Bit Score: 130.87  E-value: 1.04e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGE 93
Cdd:cd23815   1 RRIQKELADLQKNPIAGISAGPVEDNLFEWKGTILGPVGSPYEGGIFKFKITFPEDYPFKPPTVKFTTKIYHPNVDDDGS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19527004  94 ICVNVLKRD-WTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARAR 149
Cdd:cd23815  81 ICLGILKSDaWKPSIKLVSVLNALLDLLEEPNPDDALVPSIAEQYKTDRAKFNKTAR 137
UBCc_UBE2A_2B cd23790
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, ...
 23-149 2.71e-38

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, E2B and related proteins; The E2A/2B subfamily includes mammalian ubiquitin-conjugating enzymes UBE2A/RAD6A and UBE2B/RAD6B, yeast ubiquitin-conjugating enzyme E2 2 (UBC2/RAD6), plant ubiquitin-conjugating enzyme E2 1-3 (UBC1-3), and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. Both UBE2A/RAD6A and UBE2B/RAD6B are required for post-replication repair of UV-damaged DNA. In vitro, they catalyze 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. UBE2B might also catalyze 'Lys-63'-linked polyubiquitination. Saccharomyces cerevisiae UBC2 is required for DNA repair, damage-induced mutagenesis, and sporulation.


Pssm-ID: 467410  Cd Length: 143  Bit Score: 129.55  E-value: 2.71e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  23 LTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVNVLKRD 102
Cdd:cd23790  14 LQKDPPEGISAAPVEDNIMVWNAVIFGPEDTPWEGGTFKLRLEFSEEYPNKPPKVRFVSKMFHPNVYADGSICLDILQNR 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19527004 103 WTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARAR 149
Cdd:cd23790  94 WSPTYDVSAILTSIQSLLTDPNPNSPANSEAAQLYQENRREYNRRVR 140
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 14-149 3.70e-38

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, E2 M and related proteins; The E2F/E2M subfamily includes mammalian ubiquitin-conjugating enzymes E2 F (UBE2F/NCE2, EC 2.3.2.32) and E2 M (UBE2M/UBC12, EC 2.3.2.34), yeast NEDD8-conjugating enzyme UBC12 (EC 2.3.2.24), plant RUB1-conjugating enzyme 1-2 (RCE1/UBC12 and RCE2/UBC12L, EC 2.3.2.-), and similar proteins. UBE2F (also called EDD8-conjugating enzyme UBE2F, NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, or RING-type E3 NEDD8 transferase UBE2F) and UBE2M (also called NEDD8-conjugating enzyme UBC12, or NEDD8 carrier protein) accept the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. The RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. UBE2M is involved in cell proliferation. Saccharomyces cerevisiae UBC12 and Arabidopsis thaliana RCE1/RCE2 accept the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and the ECR1-AXR1 E1 complex, respectively.


Pssm-ID: 467414  Cd Length: 138  Bit Score: 129.22  E-value: 3.70e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVYKEVTTLtaDPPDGIKV-FPNEEDLTDLQVTIEGPEGtPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNG 92
Cdd:cd23794   4 LRLQKDLEEL--DLPGQCKVeFPDPNDLLKFEVTITPDEG-YYKGGTFVFEIDIPDNYPFEPPKVKCLTKIYHPNIDEEG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19527004  93 EICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARAR 149
Cdd:cd23794  81 NVCLNILREDWKPVLSLKDVILGLLFLFLEPNPDDPLNKEAAELLLRDPEEFERNVR 137
UBCc_UBE2K cd23800
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 K ...
 16-154 3.90e-37

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 K and related proteins; The E2J subfamily includes mammalian ubiquitin-conjugating enzymes E2 K (UBE2K/HIP2/LIG), yeast ubiquitin-conjugating enzyme E2 1 (UBC1), and plant ubiquitin-conjugating enzyme E2 27 (UBC27). They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2K is also called huntingtin-interacting protein 2 (HIP-2), ubiquitin-conjugating enzyme E2-25 kDa, or ubiquitin-conjugating enzyme E2(25K). In vitro, in the presence or absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, UBE2K catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. It does not transfer ubiquitin directly, but elongates monoubiquitinated substrate proteins. Saccharomyces cerevisiae UBC1, also called ubiquitin-conjugating enzyme E2-24 kDa, functions in the degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. It is a cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M).


Pssm-ID: 467420  Cd Length: 145  Bit Score: 126.90  E-value: 3.90e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  16 VYKEVTTLTADPPD--GIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGP-NG 92
Cdd:cd23800   4 IKKELKEVQKDSEAesGIKVELVGDDLTHLKGEIAGPPDTPYEGGTFVLDIKIPDTYPFEPPKMKFITKIWHPNISSqTG 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527004  93 EICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEI 154
Cdd:cd23800  84 AICLDILKDQWSPALTLRTALLSIQALLSAPEPDDPQDAVVAKQYKSNREEFEKTARHWTET 145
UBCc_UBE2D cd23792
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 18-153 2.58e-35

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 D1-D3 and related proteins; The E2D family includes mammalian ubiquitin-conjugating enzyme E2 D1-4 (UBE2D1/SFT/UBC5A/UBCH5/UBCH5A, UBE2D2/PUBC1/UBC4/UBC5B/UBCH4/UBCH5B, UBE2D3/UBC5C/UBCH5C, UBE2D4/HBUCE1/UBCH5D), yeast E2 ubiquitin-conjugating enzyme 4 (UBC4) and 5 (UBC5), as well as plant counterpart ubiquitin-conjugating enzyme E2 8-12 (UBC8/UBCAT4A, UBC9/UBCAT4B, UBC10-12) and 28-30 (UBC28-30). They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. In vitro, UBE2D1-3 (EC 2.3.2.23 and EC 2.3.2.24) catalyze 'Lys-48'-linked polyubiquitination. UBE2D3 also catalyzes 'Lys-11'-linked polyubiquitination. In vitro, UBE2D4 can promote polyubiquitination using all 7 ubiquitin Lys residues but may prefer 'Lys-11' and 'Lys-48'-linked polyubiquitination. Saccharomyces cerevisiae UBC4-5 and Arabidopsis thaliana UBC8-11 mediates the selective degradation of short-lived and abnormal proteins.


Pssm-ID: 467412  Cd Length: 143  Bit Score: 121.99  E-value: 2.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  18 KEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVN 97
Cdd:cd23792   6 KELQDLGRDPPANCSAGPVGDDLFHWQATIMGPPDSPYQGGVFFLNIHFPTDYPFKPPKVAFTTKIYHPNINSNGSICLD 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19527004  98 VLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTE 153
Cdd:cd23792  86 ILKDQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHLYKTDREKYEATAREWTR 141
UBCc_UBE2G1 cd23795
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G1 ...
 14-149 1.69e-34

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G1 and related proteins; The subfamily includes mammalian ubiquitin-conjugating enzymes E2 G1 (UBE2G1/UBC7/E217K), fission yeast ubiquitin-conjugating enzyme E2 15 (UBC15), plant ubiquitin-conjugating enzymes E2 7 (UBC7), E2 13 (UBC13) and E2 14 (UBC14). They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. In vitro, UBE2G1 catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. It may be involved in the degradation of muscle-specific proteins and may mediate polyubiquitination of CYP3A4. Schizosaccharomyces pombe UBC15 has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors. Arabidopsis thaliana UBC7, UBC13 and UBC14 are involved in the formation of multiubiquitin chains. They signal the protein for selective degradation.


Pssm-ID: 467415  Cd Length: 155  Bit Score: 120.35  E-value: 1.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVYKEVTTLTADPPDGIKV-FPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNG 92
Cdd:cd23795   4 LLLRKQLKELQKNPVEGFSAgLVDDSNIYEWEVMIIGPPDTLYEGGFFKAELTFPDDYPNSPPKMKFITEMWHPNVYPDG 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  93 EICVNVL-----------KRD--WTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARAR 149
Cdd:cd23795  84 DVCISILhppgedkngyeKASerWLPIHTVETILISVISMLSDPNDESPANVDAAKEWREDPDEFKKKVR 153
UBCc_UBE2G2 cd23796
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G2 ...
 14-153 2.17e-34

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G2 and related proteins; The subfamily includes mammalian ubiquitin-conjugating enzymes E2 G2 (UBE2G2/UBC7), yeast E2 ubiquitin-conjugating enzyme 7 (UBC7) and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. In vitro, UBE2G2 catalyzes 'Lys-48'-linked polyubiquitination. It is involved in endoplasmic reticulum-associated degradation (ERAD) and is required for sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent proteasomal degradation. UBC7, also called ubiquitin-conjugating enzyme E2-18 kDa, functions in the degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system.


Pssm-ID: 467416 [Multi-domain]  Cd Length: 158  Bit Score: 120.07  E-value: 2.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVyKEVTTLTADPPDGIKVFP-NEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNG 92
Cdd:cd23796   3 RLM-AEYKQLTLNPPEGIVAGPvSEDNFFEWEALIQGPEGTPFEGGVFPARLTFPKDYPLSPPKMKFTCEMFHPNIYPDG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527004  93 EICVNVL--------------KRdWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTE 153
Cdd:cd23796  82 RVCISILhapgddpmgyesssER-WSPVQSVEKILLSVVSMLAEPNDESGANVDAAKMWREDREEFNKIAKALVR 155
UBCc_UBE2C cd23791
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 C ...
 18-144 3.59e-34

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 C and related proteins; The E2C family includes mammalian ubiquitin-conjugating enzyme E2 C (UBE2C/UBCH10), yeast E2 ubiquitin-conjugating enzyme 11 (UBC11), plant ubiquitin-conjugating enzyme E2 19 (UBC19) and 20 (UBC20). They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2C, also known as (E3-independent) E2 ubiquitin-conjugating enzyme C (EC 2.3.2.24), E2 ubiquitin-conjugating enzyme C, ubiquitin carrier protein C, or ubiquitin-protein ligase C, catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination in vitro. It is a ubiquitin carrier protein required for the destruction of mitotic cyclins and proteins that maintain sister chromatid cohesion in animal cells and in Schizosaccharomyces pombe. In Saccharomyces cerevisiae, UBC11 is not essential for mitotic cyclin destruction. Arabidopsis thaliana UBC19 is part of the anaphase-promoting complex (APC). It may have a key function during cell cycle and be involved in cyclin B1 degradation.


Pssm-ID: 467411  Cd Length: 140  Bit Score: 118.83  E-value: 3.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  18 KEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVN 97
Cdd:cd23791   6 SELMTLMMSGDPGISAFPDGDNLFKWIGTITGPEGTVYEGLKYKLSLEFPSNYPYKAPTVKFETPCFHPNVDQHGNICLD 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19527004  98 VLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRlLLENYEEY 144
Cdd:cd23791  86 ILKEKWSALYDVRTILLSIQSLLGEPNNDSPLNGQAAE-LWDNQEEY 131
PTZ00390 PTZ00390
ubiquitin-conjugating enzyme; Provisional
 12-130 3.10e-33

ubiquitin-conjugating enzyme; Provisional


Pssm-ID: 240397  Cd Length: 152  Bit Score: 117.22  E-value: 3.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004   12 IIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN 91
Cdd:PTZ00390   3 ISKRIEKETQNLANDPPPGIKAEPDPGNYRHFKILMEGPDGTPYEGGYYKLELFLPEQYPMEPPKVRFLTKIYHPNIDKL 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19527004   92 GEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALN 130
Cdd:PTZ00390  83 GRICLDILKDKWSPALQIRTVLLSIQALLSAPEPDDPLD 121
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 16-153 6.72e-33

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 116.00  E-value: 6.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004   16 VYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEIC 95
Cdd:PLN00172   6 IQKEHKDLLKDPPSNCSAGPSDENLFRWTASIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTTKIYHPNINSNGSIC 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19527004   96 VNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTE 153
Cdd:PLN00172  86 LDILRDQWSPALTVSKVLLSISSLLTDPNPDDPLVPEIARVFKENRSRYEATAREWTQ 143
UBCc_UBE2E cd23793
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 18-152 1.11e-32

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 E1-E3 and related proteins; The E2E subfamily includes mammalian ubiquitin-conjugating enzyme E2 E1-3 (UBE2E1/UBCH6, UBE2E2/UBCH8, UBE2E3/UBCH9) and similar proteins. UBE2E, also known as (E3-independent) E2 ubiquitin-conjugating enzyme E, or E2 ubiquitin-conjugating enzyme E, accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2E1 (EC 2.3.2.23 and EC 2.3.2.24) catalyzes the covalent attachment of ISG15 to other proteins. It mediates the selective degradation of short-lived and abnormal proteins. In vitro, it also catalyzes 'Lys-48'-linked polyubiquitination. In vitro, both UBE2E2 (EC 2.3.2.23) and UBE2E3 (EC 2.3.2.23) catalyze 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. UBE2E2 catalyzes the ISGylation of influenza A virus NS1 protein. UBE2E3 participates in the regulation of trans-epithelial sodium transport in renal cells. It may be involved in cell growth arrest.


Pssm-ID: 467413  Cd Length: 141  Bit Score: 115.17  E-value: 1.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  18 KEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVN 97
Cdd:cd23793   5 KELAEITLDPPPNCSAGPKGDNLYEWVSTILGPPGSVYEGGVFFLDIHFPPDYPFKPPKVTFRTRIYHCNINSQGVICLD 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19527004  98 VLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLT 152
Cdd:cd23793  85 ILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYLTDREEHDRIAREWT 139
UBCc_ScPEX4-like cd23812
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 ...
 14-137 1.62e-32

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 (PEX4) protein and related proteins; Saccharomyces cerevisiae PEX4 (EC 2.3.2.23), also called ubiquitin-conjugating enzyme E2-21 kDa, UBC10, or PAS2, acts as a ubiquitin-conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. It is essential for peroxisome biogenesis and is required for UBC4-independent ubiquitination of PEX5. This subfamily also includes Arabidopsis thaliana PEX4 (also known as UBC21, EC 2.3.2.23) that is required for peroxisome biogenesis. It is necessary for the developmental elimination of obsolete peroxisome matrix proteins. It may be involved in the ubiquitination of PEX5, targeting it for recycling.


Pssm-ID: 467432 [Multi-domain]  Cd Length: 145  Bit Score: 114.95  E-value: 1.62e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVyKEVTTLTADPPDG-IKVFPNEE-DLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN 91
Cdd:cd23812   2 RLL-KELRELQKEPNDPdIVLGPVEDdDLFRWEAVIKGPKDTPYEGGRFELAIQVPSNYPISPPKVKFVTKIFHPNVHFK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19527004  92 -GEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLL 137
Cdd:cd23812  81 tGEICLDILKTAWSPAWTLQSVCRAILALLSDPEPDSPLNCDAGNLL 127
UBCc_UBE2I cd23798
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I ...
 24-149 3.64e-32

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.


Pssm-ID: 467418 [Multi-domain]  Cd Length: 152  Bit Score: 114.17  E-value: 3.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  24 TADP---PDGikvfpnEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVNVLK 100
Cdd:cd23798  22 VAKPvknPDG------TLDLLKWECGIPGKKGTPWEGGLYKLTMEFPEDYPSKPPKCKFDPPLFHPNVYPSGTVCLSILN 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19527004 101 --RDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARAR 149
Cdd:cd23798  96 edKDWKPSITIKQILLGIQDLLDEPNLDDPAQAEAYTLYKNNREEYERRVR 146
UBCc_ApmR795-like cd23833
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Acanthamoeba polyphaga mimivirus ...
 14-130 1.23e-30

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Acanthamoeba polyphaga mimivirus bifunctional E2/E3 enzyme R795 and related proteins; R795 (EC 2.3.2.23/EC 2.3.2.27) is a bifunctional enzyme which acts as an E2 ubiquitin-conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. It also acts as a RING-type E3 ubiquitin-protein transferase.


Pssm-ID: 467438 [Multi-domain]  Cd Length: 117  Bit Score: 109.24  E-value: 1.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGE 93
Cdd:cd23833   1 RRILRELRSLLKNPHPNIDVYPSEEDIGFWKVLMEGPEGTPYEGGVFLLYVEFPEEYPVKPPEVRFITPIYHCNINSDGR 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19527004  94 ICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALN 130
Cdd:cd23833  81 ICHSILDRNYTPDTTMREILDAVYGLLLTPEPDDPLD 117
UBCc_UBE2R cd23803
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 ...
 19-133 8.78e-27

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 R1-R2 and related proteins; The E2R subfamily includes mammalian ubiquitin-conjugating enzymes E2 R1 (UBE2R1/UBCH3/CDC34, EC 2.3.2.23 and EC 2.3.2.24), and E2 R2 (UBE2R2/UBC3B/CDC34B, EC 2.3.2.23), which accept ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2R1 catalyzes 'Lys-48'-linked polyubiquitination. It also involved in the degradation of beta-catenin. In vitro, UBE2R2 catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. It may be involved in the degradation of katenin.


Pssm-ID: 467423 [Multi-domain]  Cd Length: 170  Bit Score: 100.89  E-value: 8.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  19 EVTTLTADPPDGIKV-FPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVN 97
Cdd:cd23803   6 ELKSLQEEPVEGFRVtLVDEDNLFEWEVAIFGPPNTLYEGGYFKAHMKFPPDYPYSPPSFRFLTKMWHPNVYENGDVCIS 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 19527004  98 VL--------------KRdWTAELGIRHVLLTIKCLLIHPNPESALNEEA 133
Cdd:cd23803  86 ILhppvddpqsgelpsER-WNPTQNVRTILLSVISLLNEPNTSSPANVDA 134
UBCc_UBE2H cd23797
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 H ...
 32-149 1.57e-25

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 H and related proteins; The E2H subfamily includes mammalian ubiquitin-conjugating enzymes E2 H (UBE2H), yeast E2 ubiquitin-conjugating enzyme 8 (UBC8/GID3), and plant ubiquitin-conjugating enzyme E2 4-6 (UBC4-6). They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2H (also E3-independent, EC 2.3.2.24) transfers ubiquitin to MAEA, a core component of the CTLH E3 ubiquitin-protein ligase complex. In vitro, UBE2H catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. It might also ubiquitinate histone H2A. Saccharomyces cerevisiae UBC8 is required for the adaptation to the presence of glucose in the growth medium; it mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. It is also required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1).


Pssm-ID: 467417  Cd Length: 138  Bit Score: 96.49  E-value: 1.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  32 KVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVG-PNGEICVNVLKRDWTAE---L 107
Cdd:cd23797  16 EVTLLNDSMNEFIVKFHGPKDTPYEGGVWKVRVELPDDYPYKSPSIGFVNKIFHPNIDeASGSVCLDVINQTWSPMydlV 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19527004 108 GIRHVLLtiKCLLIHPNPESALNEEAGRLLLENYEEYAARAR 149
Cdd:cd23797  96 NIFEVFL--PQLLTYPNPSDPLNGEAAALMLHDPEAYKEKVK 135
UBCc_UBE2Z cd23809
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Z ...
 13-144 1.24e-24

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Z and related proteins; The E2Z subfamily includes mammalian ubiquitin-conjugating enzymes E2 Z (UBE2Z/HOYS7) and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2Z, also called Uba6-specific E2 conjugating enzyme 1 (Use1), acts as a ubiquitin-conjugating enzyme that accept ubiquitin from the E1 complex and catalyzes the covalent attachment to other proteins. It is a specific substrate for UBA6, not charged with ubiquitin by UBE1. It may be involved in apoptosis regulation.


Pssm-ID: 467429  Cd Length: 151  Bit Score: 94.61  E-value: 1.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  13 IRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTK-----IFHPN 87
Cdd:cd23809   1 LLRIKRDLMDIYKDPPPGIFVAPDEEDITKVHALIIGPPDTPYEGGFFYFLLRFPPDYPISPPKVRLMTTgggrvRFNPN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527004  88 VGPNGEICVNVL----KRDWTAELGIRHVLLTIKCLLihpNPESALNE-----EAGRLLLENYEEY 144
Cdd:cd23809  81 LYANGKVCLSILgtwtGPAWSPAQGLSSVLLSIQSLM---SENPYHNEpgfeqERDPEDSERYNEK 143
UBCc_UBE2U cd23806
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 U ...
 15-144 5.86e-24

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 U and related proteins; The E2U subfamily includes mammalian ubiquitin-conjugating enzymes E2 U (UBE2U/, EC 2.3.2.23) and similar proteins. They are ubiquitin-conjugating enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins.


Pssm-ID: 467426  Cd Length: 141  Bit Score: 92.68  E-value: 5.86e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  15 LVYKEVTTLTADPPDGIKVFP-NEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN-G 92
Cdd:cd23806   2 LLERELLELQENPLWGIEAKPvSDDNLFEWTAKIKGLKDTIWEGGIFRLTLKFSENYNYVPPEVQFHTIPFHPNVDPItG 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19527004  93 EICVNVLKRD--WTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEY 144
Cdd:cd23806  82 RPCIDFLDDPekWNPSYSLKSILLSIQVLLSNPVLENPVNPEAAEMLKTSPHLY 135
UBCc_UBE2W cd23808
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W ...
 18-116 1.27e-21

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W and related enzymes; The E2W subfamily includes mammalian ubiquitin-conjugating enzymes E2 W (UBE2W/UBC16), plant ubiquitin-conjugating enzyme E2 15-18 (UBC15-18), and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2W, also called FLJ11011, E2 ubiquitin-conjugating enzyme W, N-terminal E2 ubiquitin-conjugating enzyme (EC 2.3.2.25), N-terminus-conjugating E2, ubiquitin carrier protein W, ubiquitin-conjugating enzyme 16 (UBC-16), or ubiquitin-protein ligase W, specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. In vitro, UBE2W catalyzes 'Lys-11'-linked polyubiquitination. UBE2W is an important protein for early postnatal survival and for the normal functioning of multiple organ systems.


Pssm-ID: 467428 [Multi-domain]  Cd Length: 119  Bit Score: 86.04  E-value: 1.27e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  18 KEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFL-TKI-FHPNVGPNGEIC 95
Cdd:cd23808   6 KELKELQKNPPPGITLDVADNNLTEWIVTIEGAPGTLYEGEKFRLRFKFPPDYPIESPEVVFVgPPIpVHPHVYSNGHIC 85

                        90       100
                ....*....|....*....|.
gi 19527004  96 VNVLKRDWTAELGIRHVLLTI 116
Cdd:cd23808  86 LSILYDDWSPALTVSSVCLSI 106
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 14-124 1.49e-19

ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domains mostly found in non-vertebrate eukaryotes. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester 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 thioester linkages without the use of E3s.


Pssm-ID: 467440 [Multi-domain]  Cd Length: 120  Bit Score: 80.76  E-value: 1.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLV--YKEvttLTADPPDGIKVFPNEEDLTDLQVTIEGPEGtPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN 91
Cdd:cd23955   2 RLLrdLKE---LQEEPLPGVSAEPLENDLFEWHVNIRGPDG-PYSGVILHLELTFPEDYPNSPPSVRLLTPLPHPNVFTG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19527004  92 GEICVNVLK----------RDWTAELGIRHVLLTIKCLLIHPN 124
Cdd:cd23955  78 NYICLDMLEnfakhhskpySGWSPAYTVQSILLQLQAFLFDED 120
UBCc_UBE2L3 cd23801
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, ...
 13-156 2.01e-18

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, L5, L6 and related proteins; The E2L3-like subfamily includes mammalian ubiquitin-conjugating enzymes E2 L3 (UBE2L3/UBCH7/UBCE7), L5 (UBE2L5), L6 (UBE2L6/UBCH8), and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2L3 specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. It does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like RING-HECT hybrids. In vitro, UBE2L3 catalyzes 'Lys-11'-linked polyubiquitination. It is involved in the selective degradation of short-lived and abnormal proteins. In addition to ubiquitin, UBE2L6 also catalyzes the covalent attachment of ISG15 to other proteins. It functions in the E6/E6-AP-induced ubiquitination of p53/TP53. It promotes ubiquitination and subsequent proteasomal degradation of FLT3.


Pssm-ID: 467421  Cd Length: 147  Bit Score: 78.46  E-value: 2.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  13 IRLVyKEVTTLTADPPDGI-KVFPNEEDLTDLQVTIEgPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN 91
Cdd:cd23801   3 RRLQ-KELEELRKSGPKYFrDLSVDESNVLKWTGLLV-PDNPPYNKGAFRIEITFPAEYPFKPPKITFKTKIYHPNVDEK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527004  92 GEICVNVLKRD-WTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIHG 156
Cdd:cd23801  81 GQVCLPIISPEnWKPATKIDQVLQALLALINDPEPEHPLRADLAEEYSKDKKKFLKNAEEFTKKHA 146
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 53-149 2.52e-18

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and related proteins; Saccharomyces cerevisiae CDC34 (EC 2.3.2.23), also called ubiquitin-conjugating enzyme E2-34 kDa, cell division control protein 34, E2 ubiquitin-conjugating enzyme 3 (UBC3), DNA6, or ubiquitin ligase complex SCF subunit CDC34, catalyzes the covalent attachment of ubiquitin to other proteins. In vitro, it may ubiquitinate histone H2A. CDC34 mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). It is the catalytic subunit of an SCF ubiquitin-protein ligase complex (together with Skp1p, Rbx1p, CDC53, and an F-box protein) that regulates cell cycle progression by targeting key substrates for degradation. Moreover, CDC34 is involved in the regulation of methionine biosynthesis genes and in the degradation of CDC6 together with CDC4 and CDC53.


Pssm-ID: 467431  Cd Length: 170  Bit Score: 78.64  E-value: 2.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  53 TPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVNVL-------------KRDWTAELGIRHVLLTIKCL 119
Cdd:cd23811  44 SIYNGGYFKAEMVFPRDYPFSPPSFRFLPPIFHPNVYPDGRLCISILhspgddyqsgepaAERWSPAQTVESVLLSILSL 123

                        90       100       110
                ....*....|....*....|....*....|
gi 19527004 120 LIHPNPESALNEEAGRLLLENYEEYAARAR 149
Cdd:cd23811 124 LEDPNINSPANVDAGVLYRKNREEYKDKVK 153
UBCc_UBE2J cd23799
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 J1, ...
 18-114 4.89e-16

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 J1, J2 and related proteins; The E2J subfamily includes mammalian ubiquitin-conjugating enzymes E2 J1 (UBE2J1/HSPC153/HSPC205/NCUBE1) and J2 (UBE2J2/NCUBE1), yeast ubiquitin-conjugating enzyme E2 6 (UBC6/DOA2), and plant ubiquitin-conjugating enzyme E2 32-34 (UBC32-34). They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2J1 and UBE2J2 are non-canonical ubiquitin-conjugating enzyme (NCUBE), which function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). Saccharomyces cerevisiae UBC6 functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. It is a cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains.


Pssm-ID: 467419  Cd Length: 134  Bit Score: 71.73  E-value: 4.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  18 KEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTkifhpnvgPNG----- 92
Cdd:cd23799   5 KELRELQKDPPPYIVAAPLEDNILEWHFTIRGPPDTPYEGGIYHGKIVFPPDYPFKPPSIYMLT--------PNGrfetn 76

                        90       100
                ....*....|....*....|....*.
gi 19527004  93 -EICVNVL---KRDWTAELGIRHVLL 114
Cdd:cd23799  77 tKICLSISsfhPESWNPAWSIRTILI 102
UBCc_UBE2O cd23837
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 O ...
 13-153 8.43e-14

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 O and related proteins; The E2O subfamily includes mammalian ubiquitin-conjugating enzymes E2 O (UBE2O, EC 2.3.2.24), plant ubiquitin-conjugating enzyme E2 23-26 (UBC23-26, EC2.3.2.23) and E2 38-39 (UBC38-39, EC2.3.2.23), and similar proteins. UBE2O is an E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins. Arabidopsis thaliana UBC proteins accept the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBC24, also called PHO2, mediates PHO1 degradation through multivesicular body-mediated vacuolar proteolysis in response to inorganic phosphate (Pi) availability. It negatively regulates the protein abundance of PHF1 and PHT1s under Pi-sufficient conditions by facilitating the degradation of PHT1 proteins at the endomembrane.


Pssm-ID: 467439 [Multi-domain]  Cd Length: 198  Bit Score: 67.19  E-value: 8.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  13 IRLVYKEVTTLTADPPDGI--KVFPNEEDLtdLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLT----KIfHP 86
Cdd:cd23837   4 LKRVRKEWKLLKTSLPDGIfvRAYEDRMDL--LRALIVGPEGTPYEDGLFFFDIQLPPDYPNVPPKVHYHSwtggRL-NP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527004  87 NVGPNGEICVNVL------KRD-WTAEL-GIRHVLLTIKCLLIhpNPESALNeEAGRLLLENYEEYAARARLLTE 153
Cdd:cd23837  81 NLYEDGKVCLSLLgtwsgkGTEkWTPKSsNLLQVLVSIQGLVL--VKEPYYN-EAGYDKQRGTQEGRENSRMYNE 152
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 23-123 1.39e-13

ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, also called Ft1, or fused toes protein homolog, is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). AKTIP regulates apoptosis by enhancing phosphorylation and activation of AKT1. It increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. AKTIP contains a UEV domain that is homologous to E2 ubiquitin ligases but lacks the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467434  Cd Length: 112  Bit Score: 64.49  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  23 LTADPPDGIKVFPNEEDLTDLQVTIEGPEGtPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGP-NGEICVNVLKR 101
Cdd:cd23814  10 LREQPPPGVYVLPSAENPLLWHGVIFVRSG-LYKGGIFRFTISIPDNYPDGPPRVTFLSPVFHPLVDPqTGELDLSRAFP 88

                        90       100
                ....*....|....*....|...
gi 19527004 102 DWTA-ELGIRHVLLTIKCLLIHP 123
Cdd:cd23814  89 KWRPgKHHIWHVLNYLKRIFYDI 111
UBCc_TcUBE-like cd23828
Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi ...
 14-118 1.49e-13

Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi putative ubiquitin-conjugating enzyme E2 and related proteins; This subfamily includes uncharacterized Trypanosoma cruzi putative ubiquitin-conjugating enzyme E2 and similar proteins. They may function as ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins.


Pssm-ID: 467437  Cd Length: 121  Bit Score: 64.72  E-value: 1.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  14 RLVYKEVTTLTADPPDGIKVFPNEED-LTDLQVTIEGPEGT-PYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPN 91
Cdd:cd23828   8 RLLLESIKTGTEVDPAGSLIASVDSDsLFHWRVVVKPPANSiVYAGNTYELLVIFSDDYPHEPPKVRFLTPIYSPLVSPE 87

                        90       100       110
                ....*....|....*....|....*....|.
gi 19527004  92 GEICVNVLKRDWT----AELGIRHVLLTIKC 118
Cdd:cd23828  88 GSVCERLLEDDWKptqhAADAIELVLNKIFL 118
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
13-140 3.58e-13

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


Pssm-ID: 444052 [Multi-domain]  Cd Length: 146  Bit Score: 64.35  E-value: 3.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  13 IRLVYKEVTTLTADPPDgIKVFPNEEDLTDLQVTIEGP---EGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNV- 88
Cdd:COG5078  11 LANDYEELENILARGSW-IHFKATRGNPPKYEVTFNIRgiiRGGPTYGDTHRIEITLPESYPQAPPQVRWLTPIFHPNIy 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19527004  89 GPNGEICVNVLKrDWTAELGIRHVLLTIKCLLIHPN--PESALNEEAGRLLLEN 140
Cdd:COG5078  90 EAGGSVCIGRAD-HWTPSLTLDDLIISLARLLQYENyaPHSPVNLEAARWYRSN 142
UBCc_BIRC6 cd23810
Ubiquitin-conjugating enzyme E2, catalytic (UBCc)-like domain of baculoviral IAP ...
 9-99 4.05e-10

Ubiquitin-conjugating enzyme E2, catalytic (UBCc)-like domain of baculoviral IAP repeat-containing protein 6 (BIRC6) and related proteins; BIRC6, also BIR repeat-containing ubiquitin-conjugating enzyme (BRUCE), RING-type E3 ubiquitin transferase (EC 2.3.2.27) BIRC6, or ubiquitin-conjugating BIR domain enzyme apollon (APOLLON), is an anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. It has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its targets include CASP9 and DIABLO/SMAC. BIRC6 acts as an inhibitor of CASP3, CASP7, and CASP9. BIRC6 is an important regulator for the final stages of cytokinesis. It is crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification.


Pssm-ID: 467430 [Multi-domain]  Cd Length: 205  Bit Score: 57.16  E-value: 4.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004   9 PPHIIRLVyKEVTTLTADPPD----GIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLT--- 81
Cdd:cd23810   1 PARMRRLA-KELASLSTSLPLswssSIFVRVDEERMDVMKALITGPEDTPYANGCFLFDIFFPPDYPQSPPKVNLLTtgg 79

                        90       100
                ....*....|....*....|
gi 19527004  82 -KI-FHPNVGPNGEICVNVL 99
Cdd:cd23810  80 gSVrFNPNLYNDGKVCLSLL 99
UEV_UBE2V cd23807
ubiquitin E2 variant (UEV) domain of ubiquitin-conjugating enzyme E2 variant 1, 2 and related ...
 36-117 1.60e-09

ubiquitin E2 variant (UEV) domain of ubiquitin-conjugating enzyme E2 variant 1, 2 and related proteins; The E2V subfamily includes mammalian ubiquitin-conjugating enzyme E2 variant 1 (UBE2V1/CROC1/UBE2V/UEV1) and variant 2 (UBE2V2/MMS2/UEV2), yeast ubiquitin-conjugating enzyme variant MMS2, plant ubiquitin-conjugating enzyme E2 variant 1A (UEV1A/MMZ1) and variant 1B (UEV1B/MMZ2), and similar proteins. They have no ubiquitin ligase activity on their own. UBE2V1 (also called UEV-1, CROC-1, or TRAF6-regulated IKK activator 1 beta Uev1A) and UBE2V2 (also called DDVit 1, enterocyte differentiation-associated factor 1 (EDAF-1), enterocyte differentiation-promoting factor 1 (EDPF-1), MMS2 homolog, or vitamin D3-inducible protein) form heterodimers with UBE2N, respectively. Saccharomyces cerevisiae UEV MMS2 has a role in the DNA error-free postreplication repair (PRR) pathway. It forms a heterodimer with UBC13. Arabidopsis thaliana UEV1A and UEV1A form heterodimers with UBC35 or UBC36. The heterodimers possess ubiquitin-conjugating enzyme (EC 2.3.2.23) activity, catalyzing the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Members of this subfamily may mediate transcriptional activation of target genes and plays a role in the control of progress through the cell cycle and differentiation. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467427  Cd Length: 134  Bit Score: 54.03  E-value: 1.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527004  36 NEED--LTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGP-NGEICVNVLK--RDWTAELGIR 110
Cdd:cd23807  31 DDDDmtLTHWNGTIIGPPGTVFENRIYSLKIECGENYPDEPPTVRFVTKINLPCVDQsNGVVDPRKFPvlKNWQRNYTIE 110


                ....*..
gi 19527004 111 HVLLTIK 117
Cdd:cd23807 111 TVLTELR 117
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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