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Conserved domains on  [gi|1907187278|ref|XP_036009651|]
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AKT-interacting protein isoform X4 [Mus musculus]

Protein Classification

ubiquitin-conjugating enzyme E2( domain architecture ID 10642002)

ubiquitin-conjugating enzyme E2 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:  2.3.2.23
Gene Ontology:  GO:0000209|GO:0031625|GO:0061631|GO:0005524
PubMed:  19851334|36645006|32326224|19940261|26463729
SCOP:  4001046

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 72-184 1.57e-61

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: 190.07  E-value: 1.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  72 YSLLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGdCPRLLFDIPVFHPLVDPTSG 151
Cdd:cd23814     1 YELLAEYKLLREQPPPGVYVLPSAENPLLWHGVIFVRSGLYKGGIFRFTISIPDNYPDG-PPRVTFLSPVFHPLVDPQTG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907187278 152 ELDVKRAFAKWRRNHNHIWQVLMYARRVFYKID 184
Cdd:cd23814    80 ELDLSRAFPKWRPGKHHIWHVLNYLKRIFYDID 112
 
Name Accession Description Interval E-value
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 72-184 1.57e-61

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: 190.07  E-value: 1.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  72 YSLLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGdCPRLLFDIPVFHPLVDPTSG 151
Cdd:cd23814     1 YELLAEYKLLREQPPPGVYVLPSAENPLLWHGVIFVRSGLYKGGIFRFTISIPDNYPDG-PPRVTFLSPVFHPLVDPQTG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907187278 152 ELDVKRAFAKWRRNHNHIWQVLMYARRVFYKID 184
Cdd:cd23814    80 ELDLSRAFPKWRPGKHHIWHVLNYLKRIFYDID 112
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 74-217 1.14e-29

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: 109.31  E-value: 1.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278   74 LLAEFTLVVKQKLPGVYVQPSY--RSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSG 151
Cdd:smart00212   2 LLKELKELRKDPPPGFTAYPVDdeNLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKP-PKVKFITKIYHPNVDS-SG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187278  152 ELDVKRAF-AKWRRNHNhIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKVCTA 217
Cdd:smart00212  80 EICLDILKqEKWSPALT-LETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTKKYAE 145
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 74-212 1.29e-27

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: 103.81  E-value: 1.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFI-RHGLYQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDPTsGE 152
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGpDGTPYEGGVFKLSVEFPEDYPF-KPPKVKFTTKIYHPNVDSS-GE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907187278 153 --LDVKRAfAKWRRnHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSV 212
Cdd:pfam00179  80 vcLDILKD-ERWSP-ALTLEQVLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVREYV 139
 
Name Accession Description Interval E-value
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 72-184 1.57e-61

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: 190.07  E-value: 1.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  72 YSLLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGdCPRLLFDIPVFHPLVDPTSG 151
Cdd:cd23814     1 YELLAEYKLLREQPPPGVYVLPSAENPLLWHGVIFVRSGLYKGGIFRFTISIPDNYPDG-PPRVTFLSPVFHPLVDPQTG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907187278 152 ELDVKRAFAKWRRNHNHIWQVLMYARRVFYKID 184
Cdd:cd23814    80 ELDLSRAFPKWRPGKHHIWHVLNYLKRIFYDID 112
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 74-217 1.14e-29

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: 109.31  E-value: 1.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278   74 LLAEFTLVVKQKLPGVYVQPSY--RSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSG 151
Cdd:smart00212   2 LLKELKELRKDPPPGFTAYPVDdeNLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKP-PKVKFITKIYHPNVDS-SG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187278  152 ELDVKRAF-AKWRRNHNhIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKVCTA 217
Cdd:smart00212  80 EICLDILKqEKWSPALT-LETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTKKYAE 145
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 74-212 1.29e-27

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: 103.81  E-value: 1.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFI-RHGLYQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDPTsGE 152
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGpDGTPYEGGVFKLSVEFPEDYPF-KPPKVKFTTKIYHPNVDSS-GE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907187278 153 --LDVKRAfAKWRRnHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSV 212
Cdd:pfam00179  80 vcLDILKD-ERWSP-ALTLEQVLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVREYV 139
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 74-174 4.80e-14

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: 66.93  E-value: 4.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHG-LYQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDPTsGE 152
Cdd:cd00195     3 LQKELKELQKNPPPGISVEPVDDDLFHWKATIKGPEGtPYEGGVFKLDIEFPDDYPF-KPPKVRFLTPIYHPNVDPD-GE 80

                          90       100
                  ....*....|....*....|...
gi 1907187278 153 LDVKR-AFAKWRRNHNhIWQVLM 174
Cdd:cd00195    81 ICLDIlKSEGWSPALT-LRSVLL 102
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 110-208 3.82e-11

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: 59.50  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278 110 GLYQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDPTsGE-----LDvkrafAKWRRNHN---HIWQVLMyarrVFY 181
Cdd:cd23794    41 GYYKGGTFVFEIDIPDNYPF-EPPKVKCLTKIYHPNIDEE-GNvclniLR-----EDWKPVLSlkdVILGLLF----LFL 109

                          90       100
                  ....*....|....*....|....*..
gi 1907187278 182 KIDTTSPLNPEAAVLYEKDIQLFKSKV 208
Cdd:cd23794   110 EPNPDDPLNKEAAELLLRDPEEFERNV 136
UBCc_UBE2H cd23797
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 H ...
 102-212 5.46e-10

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: 56.43  E-value: 5.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278 102 FGVIFirHG----LYQDGVFKFTVYIPDNYPdGDCPRLLFDIPVFHPLVDPTSGE--LDVKrafakwrrnhNHIW----- 170
Cdd:cd23797    27 FIVKF--HGpkdtPYEGGVWKVRVELPDDYP-YKSPSIGFVNKIFHPNIDEASGSvcLDVI----------NQTWspmyd 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907187278 171 ----------QVLMYArrvfykiDTTSPLNPEAAVLYEKDIQLFKSKVVDSV 212
Cdd:cd23797    94 lvnifevflpQLLTYP-------NPSDPLNGEAAALMLHDPEAYKEKVKEYV 138
UBCc_UBE2U cd23806
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 U ...
 77-210 2.78e-09

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: 54.55  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  77 EFTLVVKQKLPGVYVQP-SYRSALVWFGVIF-IRHGLYQDGVFKFTVYIPDNY---PdgdcPRLLFD-IPvFHPLVDPTS 150
Cdd:cd23806     6 ELLELQENPLWGIEAKPvSDDNLFEWTAKIKgLKDTIWEGGIFRLTLKFSENYnyvP----PEVQFHtIP-FHPNVDPIT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907187278 151 G-----ELDVKRafaKWRRNHnHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVD 210
Cdd:cd23806    81 GrpcidFLDDPE---KWNPSY-SLKSILLSIQVLLSNPVLENPVNPEAAEMLKTSPHLYRQMVLD 141
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 77-213 2.80e-08

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: 51.91  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  77 EFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHG-LYQDGVFKFTVYIPDNYPdGDCPRLLFDIPVFHPLVDPTsGE--L 153
Cdd:cd23815     6 ELADLQKNPIAGISAGPVEDNLFEWKGTILGPVGsPYEGGIFKFKITFPEDYP-FKPPTVKFTTKIYHPNVDDD-GSicL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278 154 DVKRAFAkWRRNhNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVK 213
Cdd:cd23815    84 GILKSDA-WKPS-IKLVSVLNALLDLLEEPNPDDALVPSIAEQYKTDRAKFNKTAREWVK 141
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 74-148 1.05e-07

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: 49.56  E-value: 1.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907187278  74 LLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDP 148
Cdd:cd23955     3 LLRDLKELQEEPLPGVSAEPLENDLFEWHVNIRGPDGPYSGVILHLELTFPEDYPN-SPPSVRLLTPLPHPNVFT 76
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 74-212 3.25e-06

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: 46.28  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQK-LPGVYVQPSYRSALVW-FGVIFI-RHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLV---- 146
Cdd:cd23811     5 LMKEYKELTKPKtGPWVHIELVNDNIFTWtVGLMVLnPDSIYNGGYFKAEMVFPRDYPFSP-PSFRFLPPIFHPNVypdg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278 147 ------------DPTSGELDVKRafakwrrnhnhiWQVLMYARRVFYKI-------DTTSPLNPEAAVLYEKDIQLFKSK 207
Cdd:cd23811    84 rlcisilhspgdDYQSGEPAAER------------WSPAQTVESVLLSIlslledpNINSPANVDAGVLYRKNREEYKDK 151


                  ....*
gi 1907187278 208 VVDSV 212
Cdd:cd23811   152 VKKTV 156
UBCc_UBE2A_2B cd23790
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, ...
 74-212 6.44e-06

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: 44.81  E-value: 6.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHG-LYQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDPTsGE 152
Cdd:cd23790     7 LMRDFKRLQKDPPEGISAAPVEDNIMVWNAVIFGPEDtPWEGGTFKLRLEFSEEYPN-KPPKVRFVSKMFHPNVYAD-GS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907187278 153 --LDVKRafAKWRRNHNhIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSV 212
Cdd:cd23790    85 icLDILQ--NRWSPTYD-VSAILTSIQSLLTDPNPNSPANSEAAQLYQENRREYNRRVRECV 143
UBCc_UBE2R cd23803
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 ...
 74-199 1.61e-05

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: 44.27  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQKLPGVYVQPSYRSAL-VWFGVIFIRHG-LYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLV----- 146
Cdd:cd23803     3 LQLELKSLQEEPVEGFRVTLVDEDNLfEWEVAIFGPPNtLYEGGYFKAHMKFPPDYPYSP-PSFRFLTKMWHPNVyengd 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187278 147 -----------DPTSGELDVKRafakWRRNHNhIWQVLMYARRVFYKIDTTSPLNPEAAVLYEK 199
Cdd:cd23803    82 vcisilhppvdDPQSGELPSER----WNPTQN-VRTILLSVISLLNEPNTSSPANVDASVMYRK 140
UBCc_UBE2T cd23805
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T ...
 112-207 1.78e-05

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: 43.67  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278 112 YQDGVFKFTVYIPDNYPdGDCPRLLFDIPVFHPLVDPtSGE--LDVKRAFAK--WRRNHNhIWQVLMYARRVFYKIDTTS 187
Cdd:cd23805    42 YEGGVFKLEITIPERYP-FEPPKVRFLTPIYHPNIDS-AGRicLDILKMPPKgsWKPSLN-ISTVLTSIRLLLAEPNPDD 118

                          90       100
                  ....*....|....*....|
gi 1907187278 188 PLNPEAAVLYEKDIQLFKSK 207
Cdd:cd23805   119 PLMADIAAEYKYNRALFDAK 138
UBCc_ScPEX4-like cd23812
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 ...
 112-197 3.13e-05

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: 42.92  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278 112 YQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDPTSGE--LDV-KRAfakWrrnhNHIW---------QVLMYARrv 179
Cdd:cd23812    44 YEGGRFELAIQVPSNYPI-SPPKVKFVTKIFHPNVHFKTGEicLDIlKTA---W----SPAWtlqsvcraiLALLSDP-- 113

                          90
                  ....*....|....*...
gi 1907187278 180 fykiDTTSPLNPEAAVLY 197
Cdd:cd23812   114 ----EPDSPLNCDAGNLL 127
UBCc_UBE2L3 cd23801
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, ...
 74-214 1.15e-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: 41.48  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQKLPGVY-VQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSGE 152
Cdd:cd23801     5 LQKELEELRKSGPKYFRdLSVDESNVLKWTGLLVPDNPPYNKGAFRIEITFPAEYPFKP-PKITFKTKIYHPNVDE-KGQ 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187278 153 --LDVKRAfAKWrRNHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKV 214
Cdd:cd23801    83 vcLPIISP-ENW-KPATKIDQVLQALLALINDPEPEHPLRADLAEEYSKDKKKFLKNAEEFTKK 144
UBCc_UBE2I cd23798
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I ...
 111-151 2.89e-03

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: 37.52  E-value: 2.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907187278 111 LYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSG 151
Cdd:cd23798    49 PWEGGLYKLTMEFPEDYPSKP-PKCKFDPPLFHPNVYP-SG 87
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 74-204 6.06e-03

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: 36.45  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187278  74 LLAEFTLVVKQ-KLPGVYVQPSYRSALVWFGVIfirHG----LYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDp 148
Cdd:cd23826     6 LRRELKALHSDdPPEGISARPLDRSLLHLLATI---EGppgsPYEGGIFFLRIQIPESYPFRP-PKVRFLTKIYHPNIS- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907187278 149 TSGE--LDVkrafakwrRNHN-----HIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLF 204
Cdd:cd23826    81 RHGDicLDI--------LEHNwslalTIEKVLISIQSLLTDPYLEDPLVPEIAELYVNDREEF 135
 
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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