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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709    79 LLAEFTMVVKQKLPGVYVQPSY--RSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSG 156
Cdd:smart00212   2 LLKELKELRKDPPPGFTAYPVDdeNLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKP-PKVKFITKIYHPNVDS-SG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564394709   157 ELDVKRAF-AKWRRNHNhIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKVCTA 222
Cdd:smart00212  80 EICLDILKqEKWSPALT-LETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTKKYAE 145

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709    79 LLAEFTMVVKQKLPGVYVQPSY--RSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSG 156
Cdd:smart00212   2 LLKELKELRKDPPPGFTAYPVDdeNLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKP-PKVKFITKIYHPNVDS-SG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564394709   157 ELDVKRAF-AKWRRNHNhIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKVCTA 222
Cdd:smart00212  80 EICLDILKqEKWSPALT-LETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTKKYAE 145

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709  79 LLAEFTMVVKQKLPGVYVQPSYRSALVWFGVIFIRHG-LYQDGVFKFTVYIPDNYPDgDCPRLLFDIPVFHPLVDPTsGE 157
Cdd:cd00195    3 LQKELKELQKNPPPGISVEPVDDDLFHWKATIKGPEGtPYEGGVFKLDIEFPDDYPF-KPPKVRFLTPIYHPNVDPD-GE 80

                         90       100
                 ....*....|....*....|...
gi 564394709 158 LDVKR-AFAKWRRNHNhIWQVLM 179
Cdd:cd00195   81 ICLDIlKSEGWSPALT-LRSVLL 102

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709 107 FGVIFirHG----LYQDGVFKFTVYIPDNYPdGDCPRLLFDIPVFHPLVDPTSGE--LDVKrafakwrrnhNHIW----- 175
Cdd:cd23797   27 FIVKF--HGpkdtPYEGGVWKVRVELPDDYP-YKSPSIGFVNKIFHPNIDEASGSvcLDVI----------NQTWspmyd 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564394709 176 ----------QVLMYArrvfykiDTTSPLNPEAAVLYEKDIQLFKSKVVDSV 217
Cdd:cd23797   94 lvnifevflpQLLTYP-------NPSDPLNGEAAALMLHDPEAYKEKVKEYV 138

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709  82 EFTMVVKQKLPGVYVQPSYRSALVWFGVIFIRHG-LYQDGVFKFTVYIPDNYPdGDCPRLLFDIPVFHPLVDPTsGE--L 158
Cdd:cd23815    6 ELADLQKNPIAGISAGPVEDNLFEWKGTILGPVGsPYEGGIFKFKITFPEDYP-FKPPTVKFTTKIYHPNVDDD-GSicL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709 159 DVKRAFAkWRRNhNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVK 218
Cdd:cd23815   84 GILKSDA-WKPS-IKLVSVLNALLDLLEEPNPDDALVPSIAEQYKTDRAKFNKTAREWVK 141

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709  79 LLAEFTMVVKQK-LPGVYVQPSYRSALVW-FGVIFI-RHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLV---- 151
Cdd:cd23811    5 LMKEYKELTKPKtGPWVHIELVNDNIFTWtVGLMVLnPDSIYNGGYFKAEMVFPRDYPFSP-PSFRFLPPIFHPNVypdg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709 152 ------------DPTSGELDVKRafakwrrnhnhiWQVLMYARRVFYKI-------DTTSPLNPEAAVLYEKDIQLFKSK 212
Cdd:cd23811   84 rlcisilhspgdDYQSGEPAAER------------WSPAQTVESVLLSIlslledpNINSPANVDAGVLYRKNREEYKDK 151

                 ....*
gi 564394709 213 VVDSV 217
Cdd:cd23811  152 VKKTV 156

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709  79 LLAEFTMVVKQKLPGVYVQPSYRSALVWFGVIfirHGL----YQDGVFKFTVYIPDNYPdGDCPRLLFDIPVFHPLVDPt 154
Cdd:cd23805    3 LKRELQLLQKDPPPGISCWPKDDSLDELEAQI---QGPegtpYEGGVFKLEITIPERYP-FEPPKVRFLTPIYHPNIDS- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564394709 155 SGE--LDVKRAFAK--WRRNHNhIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSK 212
Cdd:cd23805   78 AGRicLDILKMPPKgsWKPSLN-ISTVLTSIRLLLAEPNPDDPLMADIAAEYKYNRALFDAK 138

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394709  79 LLAEFTMVVKQKLPGVY-VQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSGE 157
Cdd:cd23801    5 LQKELEELRKSGPKYFRdLSVDESNVLKWTGLLVPDNPPYNKGAFRIEITFPAEYPFKP-PKITFKTKIYHPNVDE-KGQ 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564394709 158 --LDVKRAfAKWrRNHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKV 219
Cdd:cd23801   83 vcLPIISP-ENW-KPATKIDQVLQALLALINDPEPEHPLRADLAEEYSKDKKKFLKNAEEFTKK 144

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 564394709 116 LYQDGVFKFTVYIPDNYPDGDcPRLLFDIPVFHPLVDPtSG 156
Cdd:cd23798   49 PWEGGLYKLTMEFPEDYPSKP-PKCKFDPPLFHPNVYP-SG 87