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Conserved domains on  [gi|1065001863|gb|ODV90715|]
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hypothetical protein CANCADRAFT_109937 [Tortispora caseinolytica NRRL Y-17796]

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
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 8-135 5.61e-34

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: 116.88  E-value: 5.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   8 QEIRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSGPYKGGIFHFQIHLPDDYGSVdsaAPRVKFKSHIPsHPRIDA 87
Cdd:cd23814     1 YELLAEYKLLREQPPPGVYVLPSAENPLLWHGVIFVRSGLYKGGIFRFTISIPDNYPDG---PPRVTFLSPVF-HPLVDP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1065001863  88 -SGDLDLTLLLSKHQTGPSiddpidwlqskkriYIHTLCKFIKASFKSD 135
Cdd:cd23814    77 qTGELDLSRAFPKWRPGKH--------------HIWHVLNYLKRIFYDI 111
 
Name Accession Description Interval E-value
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 8-135 5.61e-34

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: 116.88  E-value: 5.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   8 QEIRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSGPYKGGIFHFQIHLPDDYGSVdsaAPRVKFKSHIPsHPRIDA 87
Cdd:cd23814     1 YELLAEYKLLREQPPPGVYVLPSAENPLLWHGVIFVRSGLYKGGIFRFTISIPDNYPDG---PPRVTFLSPVF-HPLVDP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1065001863  88 -SGDLDLTLLLSKHQTGPSiddpidwlqskkriYIHTLCKFIKASFKSD 135
Cdd:cd23814    77 qTGELDLSRAFPKWRPGKH--------------HIWHVLNYLKRIFYDI 111
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 10-158 4.53e-16

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: 71.46  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRIDAS 88
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPDGtPYEGGVFKLSVEFPEDY---PFKPPKVKFTTKIY-HPNVDSS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  89 GDLDLTLLLSKHQTgPSIDdpidwLQSkkriYIHTLCKFIKASFKSDLLNAAPGSLYTIDRDRFETLAKA 158
Cdd:pfam00179  78 GEVCLDILKDERWS-PALT-----LEQ----VLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVRE 137
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 10-96 7.94e-11

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: 57.69  E-value: 7.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   10 IRVELANLGSHNPSGVYVI-ANHDNLYLLDGVI-FVHSGPYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRIDA 87
Cdd:smart00212   2 LLKELKELRKDPPPGFTAYpVDDENLLEWTGTIvGPPGTPYEGGVFKLTIEFPEDY---PFKPPKVKFITKIY-HPNVDS 77


                   ....*....
gi 1065001863   88 SGDLDLTLL 96
Cdd:smart00212  78 SGEICLDIL 86
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 8-110 6.28e-06

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 44.36  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   8 QEIRVELANLGSHNPSGVYVIANHDNLY-LLDGVIFVHSGPYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRID 86
Cdd:PLN00172    4 KRIQKEHKDLLKDPPSNCSAGPSDENLFrWTASIIGPSDSPYAGGVFFLSILFPPDY---PFKPPKVQFTTKI-YHPNIN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1065001863  87 ASGDLDLTLL----------------LSKHQTGPSIDDPI 110
Cdd:PLN00172   80 SNGSICLDILrdqwspaltvskvllsISSLLTDPNPDDPL 119
 
Name Accession Description Interval E-value
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 8-135 5.61e-34

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: 116.88  E-value: 5.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   8 QEIRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSGPYKGGIFHFQIHLPDDYGSVdsaAPRVKFKSHIPsHPRIDA 87
Cdd:cd23814     1 YELLAEYKLLREQPPPGVYVLPSAENPLLWHGVIFVRSGLYKGGIFRFTISIPDNYPDG---PPRVTFLSPVF-HPLVDP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1065001863  88 -SGDLDLTLLLSKHQTGPSiddpidwlqskkriYIHTLCKFIKASFKSD 135
Cdd:cd23814    77 qTGELDLSRAFPKWRPGKH--------------HIWHVLNYLKRIFYDI 111
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 10-96 3.13e-16

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: 71.17  E-value: 3.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYGsvdSAAPRVKFKSHIPsHPRIDAS 88
Cdd:cd00195     3 LQKELKELQKNPPPGISVEPVDDDLFHWKATIKGPEGtPYEGGVFKLDIEFPDDYP---FKPPKVRFLTPIY-HPNVDPD 78


                  ....*...
gi 1065001863  89 GDLDLTLL 96
Cdd:cd00195    79 GEICLDIL 86
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 10-158 4.53e-16

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: 71.46  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRIDAS 88
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPDGtPYEGGVFKLSVEFPEDY---PFKPPKVKFTTKIY-HPNVDSS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  89 GDLDLTLLLSKHQTgPSIDdpidwLQSkkriYIHTLCKFIKASFKSDLLNAAPGSLYTIDRDRFETLAKA 158
Cdd:pfam00179  78 GEVCLDILKDERWS-PALT-----LEQ----VLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVRE 137
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 10-161 1.94e-14

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: 67.32  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDAS 88
Cdd:cd23815     3 IQKELADLQKNPIAGISAGPVEDNLFEWKGTILGPVGsPYEGGIFKFKITFPEDY---PFKPPTVKFTTKI-YHPNVDDD 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1065001863  89 GDLDLTLLlskhqtgpsidDPIDWLQSKKRIYI-HTLCKFIKASFKSDLLNAAPGSLYTIDRDRFETLAKADVE 161
Cdd:cd23815    79 GSICLGIL-----------KSDAWKPSIKLVSVlNALLDLLEEPNPDDALVPSIAEQYKTDRAKFNKTAREWVK 141
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 10-96 7.94e-11

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: 57.69  E-value: 7.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   10 IRVELANLGSHNPSGVYVI-ANHDNLYLLDGVI-FVHSGPYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRIDA 87
Cdd:smart00212   2 LLKELKELRKDPPPGFTAYpVDDENLLEWTGTIvGPPGTPYEGGVFKLTIEFPEDY---PFKPPKVKFITKIY-HPNVDS 77


                   ....*....
gi 1065001863   88 SGDLDLTLL 96
Cdd:smart00212  78 SGEICLDIL 86
UBCc_UBE2T cd23805
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T ...
 10-89 7.64e-10

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: 54.84  E-value: 7.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYGSVdsaAPRVKFKSHIpSHPRIDAS 88
Cdd:cd23805     3 LKRELQLLQKDPPPGISCWPKDDSLDELEAQIQGPEGtPYEGGVFKLEITIPERYPFE---PPKVRFLTPI-YHPNIDSA 78


                  .
gi 1065001863  89 G 89
Cdd:cd23805    79 G 79
UBCc_UBE2N cd23813
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 N ...
 10-111 7.76e-08

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


Pssm-ID: 467433  Cd Length: 144  Bit Score: 49.50  E-value: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIfvhSGP----YKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRI 85
Cdd:cd23813     5 IIKETQRLLAEPVPGISATPDEDNLRYFDVVI---DGPpdspYEGGVFKLELFLPEEY---PMAPPKVRFLTKI-YHPNI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1065001863  86 DASGD--LDL------------TLLLSKHQ--TGPSIDDPID 111
Cdd:cd23813    78 DKLGRicLDIlkdkwspalqirTVLLSIQAllSAPNPDDPLA 119
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 24-85 1.80e-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: 48.02  E-value: 1.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1065001863  24 GVYVIANHDNLYLLDGVIFVHSGPYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRI 85
Cdd:cd23955    17 GVSAEPLENDLFEWHVNIRGPDGPYSGVILHLELTFPEDY---PNSPPSVRLLTPLP-HPNV 74
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 44-96 2.55e-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: 47.94  E-value: 2.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1065001863  44 HSGPYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRIDASGDLDLTLL 96
Cdd:cd23794    39 DEGYYKGGTFVFEIDIPDNY---PFEPPKVKCLTKIY-HPNIDEEGNVCLNIL 87
UBCc_UBE2S cd23804
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S ...
 13-90 7.66e-07

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


Pssm-ID: 467424  Cd Length: 146  Bit Score: 46.70  E-value: 7.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1065001863  13 ELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDASGD 90
Cdd:cd23804    10 ELQSLQSNPPEGIRVIPNEEDLTDIQAEIEGPEGtPYEGGVFRVKLVLGPDF---PASPPKGYFLTKI-FHPNVSPTGE 84
UBCc_UBE2O cd23837
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 O ...
 10-78 8.54e-07

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


Pssm-ID: 467439 [Multi-domain]  Cd Length: 198  Bit Score: 47.55  E-value: 8.54e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYGSVdsaAPRVKFKSH 78
Cdd:cd23837     7 VRKEWKLLKTSLPDGIFVRAYEDRMDLLRALIVGPEGtPYEDGLFFFDIQLPPDYPNV---PPKVHYHSW 73
UBCc_UBE2R cd23803
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 ...
 13-109 1.11e-06

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: 46.58  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  13 ELANLGSHNPSGVYV-IANHDNLYLLDGVIFvhsGP----YKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDA 87
Cdd:cd23803     6 ELKSLQEEPVEGFRVtLVDEDNLFEWEVAIF---GPpntlYEGGYFKAHMKFPPDY---PYSPPSFRFLTKM-WHPNVYE 78

                          90       100
                  ....*....|....*....|..
gi 1065001863  88 SGDLDLTLLlskHqtgPSIDDP 109
Cdd:cd23803    79 NGDVCISIL---H---PPVDDP 94
UBCc_UBE2E cd23793
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 10-96 2.39e-06

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: 45.45  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDAS 88
Cdd:cd23793     3 IQKELAEITLDPPPNCSAGPKGDNLYEWVSTILGPPGsVYEGGVFFLDIHFPPDY---PFKPPKVTFRTRI-YHCNINSQ 78


                  ....*...
gi 1065001863  89 GDLDLTLL 96
Cdd:cd23793    79 GVICLDIL 86
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 8-110 6.28e-06

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 44.36  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   8 QEIRVELANLGSHNPSGVYVIANHDNLY-LLDGVIFVHSGPYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRID 86
Cdd:PLN00172    4 KRIQKEHKDLLKDPPSNCSAGPSDENLFrWTASIIGPSDSPYAGGVFFLSILFPPDY---PFKPPKVQFTTKI-YHPNIN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1065001863  87 ASGDLDLTLL----------------LSKHQTGPSIDDPI 110
Cdd:PLN00172   80 SNGSICLDILrdqwspaltvskvllsISSLLTDPNPDDPL 119
UBCc_UBE2K cd23800
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 K ...
 23-85 1.01e-05

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: 43.70  E-value: 1.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1065001863  23 SGVYVIANHDNLYLLDGVIfvhSGP----YKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRI 85
Cdd:cd23800    19 SGIKVELVGDDLTHLKGEI---AGPpdtpYEGGTFVLDIKIPDTY---PFEPPKMKFITKI-WHPNI 78
UBCc_UBE2A_2B cd23790
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, ...
 13-96 1.07e-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: 43.65  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  13 ELANLGSHNPSGVYVIANHDNLYLLDGVIFvhsGP----YKGGIFHFQIHLPDDYGSVdsaAPRVKFKSHIpSHPRIDAS 88
Cdd:cd23790    10 DFKRLQKDPPEGISAAPVEDNIMVWNAVIF---GPedtpWEGGTFKLRLEFSEEYPNK---PPKVRFVSKM-FHPNVYAD 82


                  ....*...
gi 1065001863  89 GDLDLTLL 96
Cdd:cd23790    83 GSICLDIL 90
PTZ00390 PTZ00390
ubiquitin-conjugating enzyme; Provisional
 6-111 2.85e-05

ubiquitin-conjugating enzyme; Provisional


Pssm-ID: 240397  Cd Length: 152  Bit Score: 42.49  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863   6 IEQEIRVELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPR 84
Cdd:PTZ00390    3 ISKRIEKETQNLANDPPPGIKAEPDPGNYRHFKILMEGPDGtPYEGGYYKLELFLPEQY---PMEPPKVRFLTKI-YHPN 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1065001863  85 IDASGD--LDL------------TLLLSKHQ--TGPSIDDPID 111
Cdd:PTZ00390   79 IDKLGRicLDIlkdkwspalqirTVLLSIQAllSAPEPDDPLD 121
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 10-96 3.82e-05

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: 42.23  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSH-NPSGVYVI-ANHDNLYLLDGVIFVHSGPYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDA 87
Cdd:cd23826     6 LRRELKALHSDdPPEGISARpLDRSLLHLLATIEGPPGSPYEGGIFFLRIQIPESY---PFRPPKVRFLTKI-YHPNISR 81


                  ....*....
gi 1065001863  88 SGDLDLTLL 96
Cdd:cd23826    82 HGDICLDIL 90
UBCc_UBE2U cd23806
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 U ...
 10-115 4.09e-05

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: 41.84  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVI-ANHDNLYLLDGVIF-VHSGPYKGGIFHFQIHLPDDYGSVdsaAPRVKFKShIPSHPRIDA 87
Cdd:cd23806     3 LERELLELQENPLWGIEAKpVSDDNLFEWTAKIKgLKDTIWEGGIFRLTLKFSENYNYV---PPEVQFHT-IPFHPNVDP 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1065001863  88 sgdldltlllskhQTG-PSI---DDPIDWLQS 115
Cdd:cd23806    79 -------------ITGrPCIdflDDPEKWNPS 97
UBCc_UBE2D cd23792
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 47-157 4.37e-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: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  47 PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDASGDLDLTLLlsKHQTGPSIDdpidwlQSKKRIYIhtlCK 126
Cdd:cd23792    42 PYQGGVFFLNIHFPTDY---PFKPPKVAFTTKI-YHPNINSNGSICLDIL--KDQWSPALT------ISKVLLSI---CS 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1065001863 127 FIKASFKSDLLNAAPGSLYTIDRDRFETLAK 157
Cdd:cd23792   107 LLTDPNPDDPLVPEIAHLYKTDREKYEATAR 137
UBCc_UBE2Z cd23809
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Z ...
 13-75 1.07e-04

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


Pssm-ID: 467429  Cd Length: 151  Bit Score: 40.68  E-value: 1.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1065001863  13 ELANLGSHNPSGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYGSVdsaAPRVKF 75
Cdd:cd23809     7 DLMDIYKDPPPGIFVAPDEEDITKVHALIIGPPDtPYEGGFFYFLLRFPPDYPIS---PPKVRL 67
UBCc_ScPEX4-like cd23812
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 ...
 10-96 1.60e-04

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: 40.22  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  10 IRVELANLGSHNPSGVYVIA--NHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRID 86
Cdd:cd23812     3 LLKELRELQKEPNDPDIVLGpvEDDDLFRWEAVIKGPKDtPYEGGRFELAIQVPSNY---PISPPKVKFVTKIF-HPNVH 78

                          90
                  ....*....|.
gi 1065001863  87 -ASGDLDLTLL 96
Cdd:cd23812    79 fKTGEICLDIL 89
UBCc_BIRC6 cd23810
Ubiquitin-conjugating enzyme E2, catalytic (UBCc)-like domain of baculoviral IAP ...
 13-77 3.79e-04

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


Pssm-ID: 467430 [Multi-domain]  Cd Length: 205  Bit Score: 39.83  E-value: 3.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  13 ELANLGSHNP----SGVYVIANHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYGSVdsaAPRVKFKS 77
Cdd:cd23810    10 ELASLSTSLPlswsSSIFVRVDEERMDVMKALITGPEDtPYANGCFLFDIFFPPDYPQS---PPKVNLLT 76
UBCc_UBE2L3 cd23801
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, ...
 13-130 3.97e-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: 39.17  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  13 ELANLGSHNPSGVY-VIANHDNLYLLDGVIFVHSGPYKGGIFHFQIHLPDDYGSVdsaAPRVKFKSHIpSHPRIDASGDL 91
Cdd:cd23801     8 ELEELRKSGPKYFRdLSVDESNVLKWTGLLVPDNPPYNKGAFRIEITFPAEYPFK---PPKITFKTKI-YHPNVDEKGQV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1065001863  92 DLTLLLSKH--------Q---------TGPSIDDPI-----DWLQSKKRIYIHTLCKFIKA 130
Cdd:cd23801    84 CLPIISPENwkpatkidQvlqallaliNDPEPEHPLradlaEEYSKDKKKFLKNAEEFTKK 144
UBCc_UBE2G2 cd23796
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G2 ...
 13-164 4.43e-04

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


Pssm-ID: 467416 [Multi-domain]  Cd Length: 158  Bit Score: 39.18  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  13 ELANLGSHNPSGVyvIA---NHDNLYLLDGVIFVHSG-PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDAS 88
Cdd:cd23796     7 EYKQLTLNPPEGI--VAgpvSEDNFFEWEALIQGPEGtPFEGGVFPARLTFPKDY---PLSPPKMKFTCEM-FHPNIYPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  89 GDLDLTLLlskHQTGpsiDDPIDWLQSKKRIY-IHTLCKfIKASFKSDLLNAAPGS--------LYTIDRDRFETLAKAD 159
Cdd:cd23796    81 GRVCISIL---HAPG---DDPMGYESSSERWSpVQSVEK-ILLSVVSMLAEPNDESganvdaakMWREDREEFNKIAKAL 153


                  ....*
gi 1065001863 160 VEASI 164
Cdd:cd23796   154 VRKSL 158
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 47-169 1.29e-03

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: 38.19  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  47 PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIpSHPRIDASGDLDLTLLlskHQTGpsiDDPID-------W--LQSKK 117
Cdd:cd23811    45 IYNGGYFKAEMVFPRDY---PFSPPSFRFLPPI-FHPNVYPDGRLCISIL---HSPG---DDYQSgepaaerWspAQTVE 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1065001863 118 RIYIHTLCKFIKASFKSDLlNAAPGSLYTIDRDRFETLAKADVEASIAALPE 169
Cdd:cd23811   115 SVLLSILSLLEDPNINSPA-NVDAGVLYRKNREEYKDKVKKTVEKSKEDIPA 165
UBCc_UBE2I cd23798
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I ...
 47-158 2.06e-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: 37.13  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065001863  47 PYKGGIFHFQIHLPDDYgsvDSAAPRVKFKSHIPsHPRIDASGDLDLTLLlskhqtgpsiDDPIDWLQSkkrIYIHTLCK 126
Cdd:cd23798    49 PWEGGLYKLTMEFPEDY---PSKPPKCKFDPPLF-HPNVYPSGTVCLSIL----------NEDKDWKPS---ITIKQILL 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1065001863 127 FIkasfkSDLL---------NAAPGSLYTIDRDRFETLAKA 158
Cdd:cd23798   112 GI-----QDLLdepnlddpaQAEAYTLYKNNREEYERRVRA 147
 
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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