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Conserved domains on  [gi|223555979|ref|NP_001138633|]
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ubiquitin-conjugating enzyme E2Q-like protein 1 [Homo sapiens]

Protein Classification

ubiquitin-conjugating enzyme family protein( domain architecture ID 439)

ubiquitin-conjugating enzyme family protein similar to ubiquitin-conjugating enzyme E2 that catalyzes the covalent attachment of ubiquitin to other proteins

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, ...
 1-148 1.93e-68

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: 204.40  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARL--SDRFISVELVDESLFDWNVKLHQVDKDSVLWQDMKETNT----EFILLNLTFPDNFPFSPPFMRVLSP 74
Cdd:cd23802    4 MKELKDLMKSqsKKLGFSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKkhgyDYIELELRFPDLYPFYPPFVRVVRP 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223555979  75 RLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTH 148
Cdd:cd23802   84 RLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSARANKSPYSEAEARAAFKRLARIH 157
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 1-148 1.93e-68

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: 204.40  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARL--SDRFISVELVDESLFDWNVKLHQVDKDSVLWQDMKETNT----EFILLNLTFPDNFPFSPPFMRVLSP 74
Cdd:cd23802    4 MKELKDLMKSqsKKLGFSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKkhgyDYIELELRFPDLYPFYPPFVRVVRP 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223555979  75 RLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTH 148
Cdd:cd23802   84 RLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSARANKSPYSEAEARAAFKRLARIH 157
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 1-107 4.78e-19

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: 78.10  E-value: 4.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979     1 MKELQDIARLSDRFISVELVDES-LFDWNVKLhqVDKDSVLWQDMKetntefILLNLTFPDNFPFSPPFMRVLSPRLeNG 79
Cdd:smart00212   3 LKELKELRKDPPPGFTAYPVDDEnLLEWTGTI--VGPPGTPYEGGV------FKLTIEFPEDYPFKPPKVKFITKIY-HP 73

                           90       100
                   ....*....|....*....|....*...
gi 223555979    80 YVLDGGAICMELLTPRGWSSAYTVEAVM 107
Cdd:smart00212  74 NVDSSGEICLDILKQEKWSPALTLETVL 101
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 1-107 1.56e-14

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: 66.45  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979    1 MKELQDIARLSDRFISVELVDESLFDWNVKLHQVDkDSvLWQDMKetnteFIlLNLTFPDNFPFSPPFMRVLSPRLE-NG 79
Cdd:pfam00179   3 QKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPD-GT-PYEGGV-----FK-LSVEFPEDYPFKPPKVKFTTKIYHpNV 74

                          90       100
                  ....*....|....*....|....*...
gi 223555979   80 YVldGGAICMELLTPRGWSSAYTVEAVM 107
Cdd:pfam00179  75 DS--SGEVCLDILKDERWSPALTLEQVL 100
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 2-114 1.34e-06

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 45.51  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   2 KELQDIARLSDRFISVELVDESLFDWNVklhqvdkdSVLWQDMKETNTEFILLNLTFPDNFPFSPPFMRVLSpRLENGYV 81
Cdd:PLN00172   8 KEHKDLLKDPPSNCSAGPSDENLFRWTA--------SIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTT-KIYHPNI 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 223555979  82 LDGGAICMELLTPRgWSSAYTVEAVMRQFAASL 114
Cdd:PLN00172  79 NSNGSICLDILRDQ-WSPALTVSKVLLSISSLL 110
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
54-93 7.89e-03

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


Pssm-ID: 444052 [Multi-domain]  Cd Length: 146  Bit Score: 35.08  E-value: 7.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223555979  54 LNLTFPDNFPFSPPFMRVLSPRLENGYVLDGGAICMELLT 93
Cdd:COG5078   62 IEITLPESYPQAPPQVRWLTPIFHPNIYEAGGSVCIGRAD 101
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 1-148 1.93e-68

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: 204.40  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARL--SDRFISVELVDESLFDWNVKLHQVDKDSVLWQDMKETNT----EFILLNLTFPDNFPFSPPFMRVLSP 74
Cdd:cd23802    4 MKELKDLMKSqsKKLGFSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKkhgyDYIELELRFPDLYPFYPPFVRVVRP 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223555979  75 RLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTH 148
Cdd:cd23802   84 RLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSARANKSPYSEAEARAAFKRLARIH 157
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 1-107 4.78e-19

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: 78.10  E-value: 4.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979     1 MKELQDIARLSDRFISVELVDES-LFDWNVKLhqVDKDSVLWQDMKetntefILLNLTFPDNFPFSPPFMRVLSPRLeNG 79
Cdd:smart00212   3 LKELKELRKDPPPGFTAYPVDDEnLLEWTGTI--VGPPGTPYEGGV------FKLTIEFPEDYPFKPPKVKFITKIY-HP 73

                           90       100
                   ....*....|....*....|....*...
gi 223555979    80 YVLDGGAICMELLTPRGWSSAYTVEAVM 107
Cdd:smart00212  74 NVDSSGEICLDILKQEKWSPALTLETVL 101
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 1-109 3.76e-18

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: 75.02  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFISVELVDESLFDWNVKLhQVDKDSVlWQDmketntEFILLNLTFPDNFPFSPPFMRVLSPRlengY 80
Cdd:cd00195    4 QKELKELQKNPPPGISVEPVDDDLFHWKATI-KGPEGTP-YEG------GVFKLDIEFPDDYPFKPPKVRFLTPI----Y 71

                         90       100       110
                 ....*....|....*....|....*....|..
gi 223555979  81 ---VLDGGAICMELLTPRGWSSAYTVEAVMRQ 109
Cdd:cd00195   72 hpnVDPDGEICLDILKSEGWSPALTLRSVLLS 103
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 1-109 8.39e-17

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: 71.52  E-value: 8.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFISVELVDESLFDWNVKLHQVDkdsvlwqdmkETNTEFIL-LNLTFPDNFPFSPPFMRVLSPrLENG 79
Cdd:cd23955    4 LRDLKELQEEPLPGVSAEPLENDLFEWHVNIRGPD----------GPYSGVILhLELTFPEDYPNSPPSVRLLTP-LPHP 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 223555979  80 YVLDGGAICMELLTPR---------GWSSAYTVEAVMRQ 109
Cdd:cd23955   73 NVFTGNYICLDMLENFakhhskpysGWSPAYTVQSILLQ 111
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 1-107 1.56e-14

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: 66.45  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979    1 MKELQDIARLSDRFISVELVDESLFDWNVKLHQVDkDSvLWQDMKetnteFIlLNLTFPDNFPFSPPFMRVLSPRLE-NG 79
Cdd:pfam00179   3 QKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPD-GT-PYEGGV-----FK-LSVEFPEDYPFKPPKVKFTTKIYHpNV 74

                          90       100
                  ....*....|....*....|....*...
gi 223555979   80 YVldGGAICMELLTPRGWSSAYTVEAVM 107
Cdd:pfam00179  75 DS--SGEVCLDILKDERWSPALTLEQVL 100
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 1-108 8.74e-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: 59.76  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDiarLSD----RFISVELVDESLFDWNVKLHQVDKDSVLwqdmketNTEFILLNLTFPDNFPFSPPFMRVLSPrL 76
Cdd:cd23811    6 MKEYKE---LTKpktgPWVHIELVNDNIFTWTVGLMVLNPDSIY-------NGGYFKAEMVFPRDYPFSPPSFRFLPP-I 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 223555979  77 ENGYVLDGGAICMELLTPRG------------WSSAYTVEAVMR 108
Cdd:cd23811   75 FHPNVYPDGRLCISILHSPGddyqsgepaaerWSPAQTVESVLL 118
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 1-115 1.59e-10

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: 55.76  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFISVELVDESLFDWNVKLHQVdKDSVLwqdmkeTNTEFiLLNLTFPDNFPFSPPFMRvLSPRLENGY 80
Cdd:cd23815    4 QKELADLQKNPIAGISAGPVEDNLFEWKGTILGP-VGSPY------EGGIF-KFKITFPEDYPFKPPTVK-FTTKIYHPN 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 223555979  81 VLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLV 115
Cdd:cd23815   75 VDDDGSICLGILKSDAWKPSIKLVSVLNALLDLLE 109
UBCc_UBE2W cd23808
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W ...
 1-106 2.89e-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: 46.75  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFISVELVDESLFDWNVKLHqVDKDSVLwqdmkeTNTEFiLLNLTFPDNFPFSPP---FMRVLSPRLE 77
Cdd:cd23808    5 QKELKELQKNPPPGITLDVADNNLTEWIVTIE-GAPGTLY------EGEKF-RLRFKFPPDYPIESPevvFVGPPIPVHP 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 223555979  78 ----NGYvldggaICMELLTpRGWSSAYTVEAV 106
Cdd:cd23808   77 hvysNGH------ICLSILY-DDWSPALTVSSV 102
UBCc_ScPEX4-like cd23812
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 ...
 1-108 6.01e-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: 46.39  E-value: 6.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFIsVELV---DESLFDWNVKLHQVdkdsvlwqdmKET---NTEFiLLNLTFPDNFPFSPPFMRVLSP 74
Cdd:cd23812    4 LKELRELQKEPNDPD-IVLGpveDDDLFRWEAVIKGP----------KDTpyeGGRF-ELAIQVPSNYPISPPKVKFVTK 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 223555979  75 RLENGYVLDGGAICMELLTpRGWSSAYTVEAVMR 108
Cdd:cd23812   72 IFHPNVHFKTGEICLDILK-TAWSPAWTLQSVCR 104
UBCc_UBE2G1 cd23795
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G1 ...
 1-107 1.18e-06

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: 45.62  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFISVELVDES-LFDWNVKLhqvdkdsvlwqdMKETNT--EFILLN--LTFPDNFPFSPPFMRVLSPR 75
Cdd:cd23795    7 RKQLKELQKNPVEGFSAGLVDDSnIYEWEVMI------------IGPPDTlyEGGFFKaeLTFPDDYPNSPPKMKFITEM 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 223555979  76 LE-NGYvlDGGAICMELLTPRG------------WSSAYTVEAVM 107
Cdd:cd23795   75 WHpNVY--PDGDVCISILHPPGedkngyekaserWLPIHTVETIL 117
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 2-114 1.34e-06

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 45.51  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   2 KELQDIARLSDRFISVELVDESLFDWNVklhqvdkdSVLWQDMKETNTEFILLNLTFPDNFPFSPPFMRVLSpRLENGYV 81
Cdd:PLN00172   8 KEHKDLLKDPPSNCSAGPSDENLFRWTA--------SIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTT-KIYHPNI 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 223555979  82 LDGGAICMELLTPRgWSSAYTVEAVMRQFAASL 114
Cdd:PLN00172  79 NSNGSICLDILRDQ-WSPALTVSKVLLSISSLL 110
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 54-106 3.44e-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: 44.15  E-value: 3.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223555979  54 LNLTFPDNFPFSPPFMRVLSPRLE-NgyVLDGGAICMELLTpRGWSSAYTVEAV 106
Cdd:cd23826   53 LRIQIPESYPFRPPKVRFLTKIYHpN--ISRHGDICLDILE-HNWSLALTIEKV 103
UBCc_UBE2D cd23792
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 2-107 2.18e-05

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: 41.86  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   2 KELQDIARLSDRFISVELVDESLFDWNVKLhqvdkdsvlwqdMKETNTEF----ILLNLTFPDNFPFSPP---FM-RVLS 73
Cdd:cd23792    6 KELQDLGRDPPANCSAGPVGDDLFHWQATI------------MGPPDSPYqggvFFLNIHFPTDYPFKPPkvaFTtKIYH 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 223555979  74 PRLENgyvldGGAICMELLTPRgWSSAYTVEAVM 107
Cdd:cd23792   74 PNINS-----NGSICLDILKDQ-WSPALTISKVL 101
UBCc_TcUBE-like cd23828
Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi ...
 15-108 2.82e-05

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: 41.22  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979  15 ISVElvDESLFDWNVKLhQVDKDSVLwqdmkETNTEFILLnLTFPDNFPFSPPFMRVLSPrLENGYVLDGGAICmELLTP 94
Cdd:cd23828   28 ASVD--SDSLFHWRVVV-KPPANSIV-----YAGNTYELL-VIFSDDYPHEPPKVRFLTP-IYSPLVSPEGSVC-ERLLE 96

                         90
                 ....*....|....*
gi 223555979  95 RGWS-SAYTVEAVMR 108
Cdd:cd23828   97 DDWKpTQHAADAIEL 111
UBCc_UBE2C cd23791
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 C ...
 1-106 4.65e-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: 41.02  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFISVELVDESLFDWNVKLHQvDKDSVlWQDMKETntefilLNLTFPDNFPFSPPFMRVLSPRLE-Ng 79
Cdd:cd23791    5 QSELMTLMMSGDPGISAFPDGDNLFKWIGTITG-PEGTV-YEGLKYK------LSLEFPSNYPYKAPTVKFETPCFHpN- 75

                         90       100
                 ....*....|....*....|....*..
gi 223555979  80 yVLDGGAICMELLTPRgWSSAYTVEAV 106
Cdd:cd23791   76 -VDQHGNICLDILKEK-WSALYDVRTI 100
UBCc_UBE2A_2B cd23790
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, ...
 54-107 4.85e-05

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: 40.95  E-value: 4.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223555979  54 LNLTFPDNFPFSPPFMRVLS----PrleNGYVldGGAICMELLTPRgWSSAYTVEAVM 107
Cdd:cd23790   53 LRLEFSEEYPNKPPKVRFVSkmfhP---NVYA--DGSICLDILQNR-WSPTYDVSAIL 104
UBCc_UBE2L3 cd23801
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, ...
 2-114 5.29e-04

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: 38.02  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   2 KELQDIAR---LSDRFISVElvDESLFDWNVKLHQvdkdsvlwqDMKETNTEFILLNLTFPDNFPFSPPFMRVLSPRlen 78
Cdd:cd23801    7 KELEELRKsgpKYFRDLSVD--ESNVLKWTGLLVP---------DNPPYNKGAFRIEITFPAEYPFKPPKITFKTKI--- 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 223555979  79 gY---VLDGGAICMELLTPRGWSSAYTVEAVMRQFAASL 114
Cdd:cd23801   73 -YhpnVDEKGQVCLPIISPENWKPATKIDQVLQALLALI 110
UBCc_ApmR795-like cd23833
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Acanthamoeba polyphaga mimivirus ...
 1-106 7.18e-04

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: 37.21  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   1 MKELQDIARLSDRFISVELVDESLFDWNVKLhqvdkdsvlwqdMKETNTEF----ILLNLTFPDNFPFSPPFMRVLSPRL 76
Cdd:cd23833    4 LRELRSLLKNPHPNIDVYPSEEDIGFWKVLM------------EGPEGTPYeggvFLLYVEFPEEYPVKPPEVRFITPIY 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 223555979  77 E---NGYvldgGAICMELLTpRGWSSAYTVEAV 106
Cdd:cd23833   72 HcniNSD----GRICHSILD-RNYTPDTTMREI 99
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 11-106 7.85e-04

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: 37.54  E-value: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979  11 SDRFISVELVDESLFDwNVKLHQVDKDSVL------------WQDMKetntefILLNLTFPDNFPFSPPFMRVLSPRlen 78
Cdd:cd23794    2 ALLRLQKDLEELDLPG-QCKVEFPDPNDLLkfevtitpdegyYKGGT------FVFEIDIPDNYPFEPPKVKCLTKI--- 71

                         90       100       110
                 ....*....|....*....|....*....|.
gi 223555979  79 gY---VLDGGAICMELLTPrGWSSAYTVEAV 106
Cdd:cd23794   72 -YhpnIDEEGNVCLNILRE-DWKPVLSLKDV 100
UBCc_UBE2E cd23793
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 53-107 1.33e-03

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: 36.97  E-value: 1.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 223555979  53 LLNLTFPDNFPFSPPFMrVLSPRLENGYVLDGGAICMELLTPRgWSSAYTVEAVM 107
Cdd:cd23793   48 FLDIHFPPDYPFKPPKV-TFRTRIYHCNINSQGVICLDILKDN-WSPALTISKVL 100
UBCc_UBE2T cd23805
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T ...
 54-107 1.88e-03

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: 36.74  E-value: 1.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979  54 LNLTFPDNFPFSPPFMRVLSPRlengY---VLDGGAICMELLT--PRG-WSSAYTVEAVM 107
Cdd:cd23805   49 LEITIPERYPFEPPKVRFLTPI----YhpnIDSAGRICLDILKmpPKGsWKPSLNISTVL 104
UBCc_UBE2H cd23797
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 H ...
 5-101 4.94e-03

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: 35.24  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555979   5 QDIARL--SDRfiSVELVDESLFDWNVKLHQvDKDSV----LWQdmketntefilLNLTFPDNFPFSPP---FM-RVLSP 74
Cdd:cd23797    5 TDVMKLmmSDY--EVTLLNDSMNEFIVKFHG-PKDTPyeggVWK-----------VRVELPDDYPYKSPsigFVnKIFHP 70

                         90       100
                 ....*....|....*....|....*..
gi 223555979  75 RLENGyvldGGAICMELLTpRGWSSAY 101
Cdd:cd23797   71 NIDEA----SGSVCLDVIN-QTWSPMY 92
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
54-93 7.89e-03

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


Pssm-ID: 444052 [Multi-domain]  Cd Length: 146  Bit Score: 35.08  E-value: 7.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223555979  54 LNLTFPDNFPFSPPFMRVLSPRLENGYVLDGGAICMELLT 93
Cdd:COG5078   62 IEITLPESYPQAPPQVRWLTPIFHPNIYEAGGSVCIGRAD 101
 
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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