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Conserved domains on  [gi|51895908|gb|AAH82275|]
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Ube2q1 protein [Mus musculus]

Protein Classification

ubiquitin-conjugating enzyme E2 variant( domain architecture ID 10076510)

ubiquitin-conjugating enzyme E2 variant lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways; similar to Caenorhabditis elegans ubiquitin-conjugating enzyme E2 variant 3 (UBE2V3)

CATH:  3.10.110.10
PubMed:  19851334|36645006|32326224|19940261|26463729
SCOP:  4001046

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 85-240 2.27e-84

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, Q2, and related proteins; The E2Q subfamily includes mammalian ubiquitin-conjugating enzymes E2 Q1 (UBE2Q1/NICE5/UBE2Q), Q2 (UBE2Q2), and similar proteins. They are ubiquitin-conjugating (EC 2.3.2.23) enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2Q1 may be involved in hormonal homeostasis in females. It is involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation. In vitro, UBE2Q2 catalyzes 'Lys-48'-linked polyubiquitination. This subfamily also includes ubiquitin-conjugating enzyme E2Q-like protein 1 (UBE2QL1), which is a probable E2 ubiquitin-protein ligase that may facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7.


:

Pssm-ID: 467422  Cd Length: 157  Bit Score: 248.70  E-value: 2.27e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  85 DRLMKELRDIYRSQSFKGGnYAVELVNDSLYDWNVKLLKVDQDSALHNDLQILKEKEGADFILLNFSFKDNFPFDPPFVR 164
Cdd:cd23802   1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51895908 165 VVSPVLSGGYVLGGGAICMELLTKQGWSSAYSIESVIMQISATLVKGKARVQFGA--NKSQYSLTRAQQSYKSLVQIH 240
Cdd:cd23802  80 VVRPRLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSAraNKSPYSEAEARAAFKRLARIH 157
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 85-240 2.27e-84

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, Q2, and related proteins; The E2Q subfamily includes mammalian ubiquitin-conjugating enzymes E2 Q1 (UBE2Q1/NICE5/UBE2Q), Q2 (UBE2Q2), and similar proteins. They are ubiquitin-conjugating (EC 2.3.2.23) enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2Q1 may be involved in hormonal homeostasis in females. It is involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation. In vitro, UBE2Q2 catalyzes 'Lys-48'-linked polyubiquitination. This subfamily also includes ubiquitin-conjugating enzyme E2Q-like protein 1 (UBE2QL1), which is a probable E2 ubiquitin-protein ligase that may facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7.


Pssm-ID: 467422  Cd Length: 157  Bit Score: 248.70  E-value: 2.27e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  85 DRLMKELRDIYRSQSFKGGnYAVELVNDSLYDWNVKLLKVDQDSALHNDLQILKEKEGADFILLNFSFKDNFPFDPPFVR 164
Cdd:cd23802   1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51895908 165 VVSPVLSGGYVLGGGAICMELLTKQGWSSAYSIESVIMQISATLVKGKARVQFGA--NKSQYSLTRAQQSYKSLVQIH 240
Cdd:cd23802  80 VVRPRLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSAraNKSPYSEAEARAAFKRLARIH 157
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 86-240 2.51e-20

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: 84.27  E-value: 2.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908     86 RLMKELRDIYRSQSFkgGNYAVELVNDSLYDWNVKLlkVDQDSALHNDLqilkekegadFILLNFSFKDNFPFDPPFVRV 165
Cdd:smart00212   1 RLLKELKELRKDPPP--GFTAYPVDDENLLEWTGTI--VGPPGTPYEGG----------VFKLTIEFPEDYPFKPPKVKF 66

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51895908    166 VSPVLsGGYVLGGGAICMELLTKQGWSSAYSIESVIMQISATLVKGKARvqFGANKSQYSLTRA-QQSYKSLVQIH 240
Cdd:smart00212  67 ITKIY-HPNVDSSGEICLDILKQEKWSPALTLETVLLSLQSLLSEPNPD--SPLNADAAELYKKnREEFKKKAREW 139
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 86-208 2.62e-11

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: 59.51  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908    86 RLMKELRDIYRSQSFkggNYAVELVNDSLYDWNVKLLKVDqDSALhndlqilkekEGADFILlNFSFKDNFPFDPPFVRV 165
Cdd:pfam00179   1 RLQKELKELLKDPPP---GISAGPVDDNLFEWKVTIIGPD-GTPY----------EGGVFKL-SVEFPEDYPFKPPKVKF 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 51895908   166 VSPVlsggY---VLGGGAICMELLTKQGWSSAYSIESVIMQISATL 208
Cdd:pfam00179  66 TTKI----YhpnVDSSGEVCLDILKDERWSPALTLEQVLLSIQSLL 107
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 83-231 9.52e-10

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 55.53  E-value: 9.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908   83 ATDRLMKELRDIYRSQSfkgGNYAVELVNDSLYDWNVKLLKvDQDSALhndlqilkekEGADFiLLNFSFKDNFPFDPPF 162
Cdd:PLN00172   2 ATKRIQKEHKDLLKDPP---SNCSAGPSDENLFRWTASIIG-PSDSPY----------AGGVF-FLSILFPPDYPFKPPK 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51895908  163 VRVVSPVLSGGyVLGGGAICMELLTKQgWSSAYSIESVIMQISA---------TLVKGKARVqFGANKSQYSLTrAQQ 231
Cdd:PLN00172  67 VQFTTKIYHPN-INSNGSICLDILRDQ-WSPALTVSKVLLSISSlltdpnpddPLVPEIARV-FKENRSRYEAT-ARE 140
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 85-240 2.27e-84

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, Q2, and related proteins; The E2Q subfamily includes mammalian ubiquitin-conjugating enzymes E2 Q1 (UBE2Q1/NICE5/UBE2Q), Q2 (UBE2Q2), and similar proteins. They are ubiquitin-conjugating (EC 2.3.2.23) enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2Q1 may be involved in hormonal homeostasis in females. It is involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation. In vitro, UBE2Q2 catalyzes 'Lys-48'-linked polyubiquitination. This subfamily also includes ubiquitin-conjugating enzyme E2Q-like protein 1 (UBE2QL1), which is a probable E2 ubiquitin-protein ligase that may facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7.


Pssm-ID: 467422  Cd Length: 157  Bit Score: 248.70  E-value: 2.27e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  85 DRLMKELRDIYRSQSFKGGnYAVELVNDSLYDWNVKLLKVDQDSALHNDLQILKEKEGADFILLNFSFKDNFPFDPPFVR 164
Cdd:cd23802   1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51895908 165 VVSPVLSGGYVLGGGAICMELLTKQGWSSAYSIESVIMQISATLVKGKARVQFGA--NKSQYSLTRAQQSYKSLVQIH 240
Cdd:cd23802  80 VVRPRLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSAraNKSPYSEAEARAAFKRLARIH 157
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 86-240 2.51e-20

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: 84.27  E-value: 2.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908     86 RLMKELRDIYRSQSFkgGNYAVELVNDSLYDWNVKLlkVDQDSALHNDLqilkekegadFILLNFSFKDNFPFDPPFVRV 165
Cdd:smart00212   1 RLLKELKELRKDPPP--GFTAYPVDDENLLEWTGTI--VGPPGTPYEGG----------VFKLTIEFPEDYPFKPPKVKF 66

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51895908    166 VSPVLsGGYVLGGGAICMELLTKQGWSSAYSIESVIMQISATLVKGKARvqFGANKSQYSLTRA-QQSYKSLVQIH 240
Cdd:smart00212  67 ITKIY-HPNVDSSGEICLDILKQEKWSPALTLETVLLSLQSLLSEPNPD--SPLNADAAELYKKnREEFKKKAREW 139
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 86-208 7.49e-19

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: 79.26  E-value: 7.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYRSQSFkggNYAVELVNDSLYDWNVkLLKVDQDSALhndlqilkekEGAdFILLNFSFKDNFPFDPPFVRV 165
Cdd:cd00195   2 RLQKELKELQKNPPP---GISVEPVDDDLFHWKA-TIKGPEGTPY----------EGG-VFKLDIEFPDDYPFKPPKVRF 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51895908 166 VSPVlsggY---VLGGGAICMELLTKQGWSSAYSIESVIMQISATL 208
Cdd:cd00195  67 LTPI----YhpnVDPDGEICLDILKSEGWSPALTLRSVLLSIQSLL 108
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 86-209 1.56e-14

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: 68.05  E-value: 1.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYRSQSFkggNYAVELVNDSLYDWNVKLLKVD---QDSALHndlqilkekegadFILLnfsFKDNFPFDPPF 162
Cdd:cd23955   2 RLLRDLKELQEEPLP---GVSAEPLENDLFEWHVNIRGPDgpySGVILH-------------LELT---FPEDYPNSPPS 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51895908 163 VRVVSPVLSGGyVLGGGAICMELLT---------KQGWSSAYSIESVIMQISATLV 209
Cdd:cd23955  63 VRLLTPLPHPN-VFTGNYICLDMLEnfakhhskpYSGWSPAYTVQSILLQLQAFLF 117
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 83-208 2.65e-12

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: 63.23  E-value: 2.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  83 ATDRLMKELRDIyrSQSFKGGNYAVELVNDSLYDWNVKLLKVDQDSALHNdlQILKEKegadfillnFSFKDNFPFDPPF 162
Cdd:cd23811   1 AAKILMKEYKEL--TKPKTGPWVHIELVNDNIFTWTVGLMVLNPDSIYNG--GYFKAE---------MVFPRDYPFSPPS 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51895908 163 VRVVSPVLSGGyVLGGGAICMELLTKQG------------WSSAYSIESVIMQISATL 208
Cdd:cd23811  68 FRFLPPIFHPN-VYPDGRLCISILHSPGddyqsgepaaerWSPAQTVESVLLSILSLL 124
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 86-208 2.62e-11

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: 59.51  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908    86 RLMKELRDIYRSQSFkggNYAVELVNDSLYDWNVKLLKVDqDSALhndlqilkekEGADFILlNFSFKDNFPFDPPFVRV 165
Cdd:pfam00179   1 RLQKELKELLKDPPP---GISAGPVDDNLFEWKVTIIGPD-GTPY----------EGGVFKL-SVEFPEDYPFKPPKVKF 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 51895908   166 VSPVlsggY---VLGGGAICMELLTKQGWSSAYSIESVIMQISATL 208
Cdd:pfam00179  66 TTKI----YhpnVDSSGEVCLDILKDERWSPALTLEQVLLSIQSLL 107
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 83-231 9.52e-10

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 55.53  E-value: 9.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908   83 ATDRLMKELRDIYRSQSfkgGNYAVELVNDSLYDWNVKLLKvDQDSALhndlqilkekEGADFiLLNFSFKDNFPFDPPF 162
Cdd:PLN00172   2 ATKRIQKEHKDLLKDPP---SNCSAGPSDENLFRWTASIIG-PSDSPY----------AGGVF-FLSILFPPDYPFKPPK 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51895908  163 VRVVSPVLSGGyVLGGGAICMELLTKQgWSSAYSIESVIMQISA---------TLVKGKARVqFGANKSQYSLTrAQQ 231
Cdd:PLN00172  67 VQFTTKIYHPN-INSNGSICLDILRDQ-WSPALTVSKVLLSISSlltdpnpddPLVPEIARV-FKENRSRYEAT-ARE 140
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 86-209 3.60e-09

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: 53.83  E-value: 3.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYRSQSfkgGNYAVELVNDSLYDWNVKLLKVdQDSALhndlqilkekEGADFiLLNFSFKDNFPFDPPFVRV 165
Cdd:cd23815   2 RIQKELADLQKNPI---AGISAGPVEDNLFEWKGTILGP-VGSPY----------EGGIF-KFKITFPEDYPFKPPTVKF 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51895908 166 VSPVlsggY---VLGGGAICMELLTKQGWSSAYSIESVIMQISATLV 209
Cdd:cd23815  67 TTKI----YhpnVDDDGSICLGILKSDAWKPSIKLVSVLNALLDLLE 109
UBCc_TcUBE-like cd23828
Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi ...
 86-204 5.32e-08

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: 50.08  E-value: 5.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELR----DIYRSQSFKGGNYAVELVN-DSLYDWNVKLlkvdqdSALHNDLQilkeKEGADFILLnFSFKDNFPFDP 160
Cdd:cd23828   2 RIGKDLRllleSIKTGTEVDPAGSLIASVDsDSLFHWRVVV------KPPANSIV----YAGNTYELL-VIFSDDYPHEP 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 51895908 161 PFVRVVSPVLSGGyVLGGGAICMELLTKqGWSSAYSIESVIMQI 204
Cdd:cd23828  71 PKVRFLTPIYSPL-VSPEGSVCERLLED-DWKPTQHAADAIELV 112
UBCc_UBE2W cd23808
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W ...
 86-204 3.16e-07

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: 47.91  E-value: 3.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIyrsQSFKGGNYAVELVNDSLYDWNVKLlKVDQDSALHNDlqilkekegaDFiLLNFSFKDNFPFDPP---F 162
Cdd:cd23808   3 RLQKELKEL---QKNPPPGITLDVADNNLTEWIVTI-EGAPGTLYEGE----------KF-RLRFKFPPDYPIESPevvF 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51895908 163 VRVVSP----VLSGGYvlgggaICMELLTkQGWSSAYSIESVIMQI 204
Cdd:cd23808  68 VGPPIPvhphVYSNGH------ICLSILY-DDWSPALTVSSVCLSI 106
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 86-204 3.52e-07

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: 48.33  E-value: 3.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYrsqsfKGGNYAVELVNDSlydwNVKLLKVdqdsalhndlqILKEKEG----ADFILlNFSFKDNFPFDPP 161
Cdd:cd23794   5 RLQKDLEELD-----LPGQCKVEFPDPN----DLLKFEV-----------TITPDEGyykgGTFVF-EIDIPDNYPFEPP 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51895908 162 FVRVVSPVlsggY---VLGGGAICMELLtKQGWSSAYSIESVIMQI 204
Cdd:cd23794  64 KVKCLTKI----YhpnIDEEGNVCLNIL-REDWKPVLSLKDVILGL 104
UBCc_UBE2K cd23800
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 K ...
 86-208 4.26e-07

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: 47.94  E-value: 4.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYRSQSFKGGnYAVELVNDSLYDWnVKLLKVDQDSALhndlqilkekEGADFILlNFSFKDNFPFDPPFVRV 165
Cdd:cd23800   3 RIKKELKEVQKDSEAESG-IKVELVGDDLTHL-KGEIAGPPDTPY----------EGGTFVL-DIKIPDTYPFEPPKMKF 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51895908 166 VSPV----LSGgyvlGGGAICMELLTKQgWSSAYSIESVIMQISATL 208
Cdd:cd23800  70 ITKIwhpnISS----QTGAICLDILKDQ-WSPALTLRTALLSIQALL 111
UBCc_ScPEX4-like cd23812
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 ...
 86-208 7.06e-07

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: 47.54  E-value: 7.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYRSQSFKGgnyaVELV---NDSLYDWNVKLLKVDqDSALhndlqilkekEGADFiLLNFSFKDNFPFDPPF 162
Cdd:cd23812   2 RLLKELRELQKEPNDPD----IVLGpveDDDLFRWEAVIKGPK-DTPY----------EGGRF-ELAIQVPSNYPISPPK 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51895908 163 VRVVSPVLSGGYVLGGGAICMELLtKQGWSSAYSIESVIMQISATL 208
Cdd:cd23812  66 VKFVTKIFHPNVHFKTGEICLDIL-KTAWSPAWTLQSVCRAILALL 110
UBCc_UBE2A_2B cd23790
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, ...
 82-204 9.15e-07

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: 47.12  E-value: 9.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  82 QATDRLMKELRDIyrsQSFKGGNYAVELVNDSLYDWNVKLLKVDqDSALhndlqilkekEGADFILLnFSFKDNFPFDPP 161
Cdd:cd23790   2 AARRRLMRDFKRL---QKDPPEGISAAPVEDNIMVWNAVIFGPE-DTPW----------EGGTFKLR-LEFSEEYPNKPP 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51895908 162 FVRVVSPVlsggY---VLGGGAICMELLTKQgWSSAYSIESVIMQI 204
Cdd:cd23790  67 KVRFVSKM----FhpnVYADGSICLDILQNR-WSPTYDVSAILTSI 107
UBCc_UBE2D cd23792
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 86-208 3.22e-06

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: 45.72  E-value: 3.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYR---SQSFKGGnyavelVNDSLYDWNVKLLKVDqDSALhndlqilkekEGADFiLLNFSFKDNFPFDPPF 162
Cdd:cd23792   3 RINKELQDLGRdppANCSAGP------VGDDLFHWQATIMGPP-DSPY----------QGGVF-FLNIHFPTDYPFKPPK 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51895908 163 V----RVVSPVLSggyvlGGGAICMELLTKQgWSSAYSIESVIMQISATL 208
Cdd:cd23792  65 VafttKIYHPNIN-----SNGSICLDILKDQ-WSPALTISKVLLSICSLL 108
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 141-208 9.11e-06

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: 44.54  E-value: 9.11e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51895908 141 EGADFiLLNFSFKDNFPFDPPFVRVVSPVlsggY---VLGGGAICMELLTKQgWSSAYSIESVIMQISATL 208
Cdd:cd23826  47 EGGIF-FLRIQIPESYPFRPPKVRFLTKI----YhpnISRHGDICLDILEHN-WSLALTIEKVLISIQSLL 111
UBCc_UBE2L3 cd23801
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, ...
 83-208 6.46e-05

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: 41.87  E-value: 6.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  83 ATDRLMKELRDIYRSqsFKGGNYAVELVNDSLYDWNVKLLKvdqDSALHNdlqilkekEGAdFILlNFSFKDNFPFDPPF 162
Cdd:cd23801   1 ASRRLQKELEELRKS--GPKYFRDLSVDESNVLKWTGLLVP---DNPPYN--------KGA-FRI-EITFPAEYPFKPPK 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 51895908 163 VRVVSPVlsggY---VLGGGAICMELLTKQGWSSAYSIESVIMQISATL 208
Cdd:cd23801  66 ITFKTKI----YhpnVDEKGQVCLPIISPENWKPATKIDQVLQALLALI 110
UBCc_UBE2C cd23791
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 C ...
 148-208 8.91e-05

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: 41.40  E-value: 8.91e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51895908 148 LNFSFKDNFPFDPPFVRVVSPVlsggY---VLGGGAICMELLtKQGWSSAYSIESVIMQISATL 208
Cdd:cd23791  50 LSLEFPSNYPYKAPTVKFETPC----FhpnVDQHGNICLDIL-KEKWSALYDVRTILLSIQSLL 108
UBCc_UBE2T cd23805
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T ...
 148-204 2.02e-04

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: 40.59  E-value: 2.02e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51895908 148 LNFSFKDNFPFDPPFVRVVSPVlsggY---VLGGGAICMELLT---KQGWSSAYSIESVIMQI 204
Cdd:cd23805  49 LEITIPERYPFEPPKVRFLTPI----YhpnIDSAGRICLDILKmppKGSWKPSLNISTVLTSI 107
UBCc_UBE2E cd23793
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 86-208 3.38e-04

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: 39.67  E-value: 3.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51895908  86 RLMKELRDIYRSQSfkgGNYAVELVNDSLYDWNVKLLKVDqDSALhndlqilkekEGADFiLLNFSFKDNFPFDPPFVRV 165
Cdd:cd23793   2 RIQKELAEITLDPP---PNCSAGPKGDNLYEWVSTILGPP-GSVY----------EGGVF-FLDIHFPPDYPFKPPKVTF 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51895908 166 VSPVlsggY---VLGGGAICMELLtKQGWSSAYSIESVIMQISATL 208
Cdd:cd23793  67 RTRI----YhcnINSQGVICLDIL-KDNWSPALTISKVLLSICSLL 107
 
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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