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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  837 VQQEWNILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPP-----SAYYHsgglrvnPNL 911
Cdd:pfam00179    2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPDGTPYEGGVFKLSVEFPEDYPFKPPkvkftTKIYH-------PNV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002233178  912 YVDGKVCLSLLNTWTgrgnevWDPsSSSILQVLVSLQGLVL---NEKPYFNEAGYEKQVGTVEGEKNA 976
Cdd:pfam00179   75 DSSGEVCLDILKDER------WSP-ALTLEQVLLSIQSLLSepnPEDPLNAEAAKLYRKNREEFEKKV 135

ubiquitin conjugating enzyme; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  835 KKVQQEWNILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAYYHSgglRV-NPNLYV 913
Cdd:PLN00172     4 KRIQKEHKDLLKDPPSNCSAGPSDENLFRWTASIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTT---KIyHPNINS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1002233178  914 DGKVCLSLLntwtgrgNEVWDPsSSSILQVLVSLQGLVLNEKP 956
Cdd:PLN00172    81 NGSICLDIL-------RDQWSP-ALTVSKVLLSISSLLTDPNP 115

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  834 VKKVQQEWNILEKNLPDY----IYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAYYHS---GGLR 906
Cdd:cd23810      4 MRRLAKELASLSTSLPLSwsssIFVRVDEERMDVMKALITGPEDTPYANGCFLFDIFFPPDYPQSPPKVNLLTtggGSVR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  907 VNPNLYVDGKVCLSLLNTWTGRGNEVWDPSSSSILQVLVSLQGLVLNEKPYFNEAGYEKQVGTVEGEKNALPYNENTYLL 986
Cdd:cd23810     84 FNPNLYNDGKVCLSLLGTWSGPPGEKWNPGTSTLLQVLVSIQSLILVPEPYFNEPGYERSRGTPEGDAASREYNANIRYN 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1002233178  987 SLK-SMLYILRRPPMHFEDFAKSHFSKRGKYILKACEAYLQ 1026
Cdd:cd23810    164 TVRwAMLEQLRNPPPGFEDVIRTHFYLKREEILAQCEKWIA 204

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 1002233178  835 KKVQQEWNILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAY-----YHsgglrvnP 909
Cdd:cd00195      1 KRLQKELKELQKNPPPGISVEPVDDDLFHWKATIKGPEGTPYEGGVFKLDIEFPDDYPFKPPKVRfltpiYH-------P 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1002233178  910 NLYVDGKVCLSLLNTwtgrgnEVWDPsSSSILQVLVSLQGLVLNE 954
Cdd:cd00195     74 NVDPDGEICLDILKS------EGWSP-ALTLRSVLLSIQSLLSDP 111

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 1002233178   844 LEKNLPDYIYVRVFED-RMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAYYHSGglRVNPNLYVDGKVCLSLL 922
Cdd:smart00212    9 LRKDPPPGFTAYPVDDeNLLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKPPKVKFITK--IYHPNVDSSGEICLDIL 86

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1002233178   923 NTwtgrgnEVWDPsSSSILQVLVSLQGLVLNEKP 956
Cdd:smart00212   87 KQ------EKWSP-ALTLETVLLSLQSLLSEPNP 113

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 1002233178  837 VQQEWNILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSA-----YYHsgglrvnPNL 911
Cdd:cd23805      3 LKRELQLLQKDPPPGISCWPKDDSLDELEAQIQGPEGTPYEGGVFKLEITIPERYPFEPPKVrfltpIYH-------PNI 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1002233178  912 YVDGKVCLSLLNTW-TGRgnevWDPsSSSILQVLVSLQgLVLNE 954
Cdd:cd23805     76 DSAGRICLDILKMPpKGS----WKP-SLNISTVLTSIR-LLLAE 113

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  835 KKVQQEW-NILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAY-----YHsgglrvn 908
Cdd:cd23826      4 RRLRRELkALHSDDPPEGISARPLDRSLLHLLATIEGPPGSPYEGGIFFLRIQIPESYPFRPPKVRfltkiYH------- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1002233178  909 PNLYVDGKVCLSLLntwtgrgNEVWDPsSSSILQVLVSLQGL 950
Cdd:cd23826     77 PNISRHGDICLDIL-------EHNWSL-ALTIEKVLISIQSL 110

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        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  861 MDLIR--AVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAY-----YHsgglrvnPNLYVDGKVCLSLLNTWTGrgnevW 933
Cdd:cd23798     33 LDLLKweCGIPGKKGTPWEGGLYKLTMEFPEDYPSKPPKCKfdpplFH-------PNVYPSGTVCLSILNEDKD-----W 100

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1002233178  934 DPsSSSILQVLVSLQGLvLNEK---------PYF----NEAGYEKQV 967
Cdd:cd23798    101 KP-SITIKQILLGIQDL-LDEPnlddpaqaeAYTlyknNREEYERRV 145

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Acanthamoeba polyphaga mimivirus bifunctional E2/E3 enzyme R795 and related proteins; R795 (EC 2.3.2.23/EC 2.3.2.27) is a bifunctional enzyme which acts as an E2 ubiquitin-conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. It also acts as a RING-type E3 ubiquitin-protein transferase.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  835 KKVQQEWNILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPP-----SAYYHsgglrvnP 909
Cdd:cd23833      1 RRILRELRSLLKNPHPNIDVYPSEEDIGFWKVLMEGPEGTPYEGGVFLLYVEFPEEYPVKPPevrfiTPIYH-------C 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1002233178  910 NLYVDGKVCLSLLNT-WTgrgnevwdpSSSSILQVLVSLQGLVLNEKP 956
Cdd:cd23833     74 NINSDGRICHSILDRnYT---------PDTTMREILDAVYGLLLTPEP 112

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  865 RAVIIGASGTPYQDGLFFFDFHLPPEFPQVPP-----SAYYHSgglRVNPNlyvdGKVCLSLLntwtgrgNEVWDPsSSS 939
Cdd:cd23793     31 VSTILGPPGSVYEGGVFFLDIHFPPDYPFKPPkvtfrTRIYHC---NINSQ----GVICLDIL-------KDNWSP-ALT 95

                           90
                   ....*....|....*...
gi 1002233178  940 ILQVLVSLQGLVLNEKPY 957
Cdd:cd23793     96 ISKVLLSICSLLTDCNPA 113

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W and related enzymes; The E2W subfamily includes mammalian ubiquitin-conjugating enzymes E2 W (UBE2W/UBC16), plant ubiquitin-conjugating enzyme E2 15-18 (UBC15-18), and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2W, also called FLJ11011, E2 ubiquitin-conjugating enzyme W, N-terminal E2 ubiquitin-conjugating enzyme (EC 2.3.2.25), N-terminus-conjugating E2, ubiquitin carrier protein W, ubiquitin-conjugating enzyme 16 (UBC-16), or ubiquitin-protein ligase W, specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. In vitro, UBE2W catalyzes 'Lys-11'-linked polyubiquitination. UBE2W is an important protein for early postnatal survival and for the normal functioning of multiple organ systems.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  835 KKVQQEWNILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAYYHSGGLRVNPNLYVD 914
Cdd:cd23808      2 KRLQKELKELQKNPPPGITLDVADNNLTEWIVTIEGAPGTLYEGEKFRLRFKFPPDYPIESPEVVFVGPPIPVHPHVYSN 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1002233178  915 GKVCLSLLntwtgrGNEvWDPsSSSILQVLVSLQ 948
Cdd:cd23808     82 GHICLSIL------YDD-WSP-ALTVSSVCLSIL 107

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  865 RAVIIGASGTPYQDGLFFFDFHLPPEFPQVPP-----SAYYHsgglrvnPNLYVDGKVCLSLLntwtgrgNEVWDPsSSS 939
Cdd:cd23792     32 QATIMGPPDSPYQGGVFFLNIHFPTDYPFKPPkvaftTKIYH-------PNINSNGSICLDIL-------KDQWSP-ALT 96

                           90
                   ....*....|....*..
gi 1002233178  940 ILQVLVSLQGLVLNEKP 956
Cdd:cd23792     97 ISKVLLSICSLLTDPNP 113

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  856 VFEDRMDLIR-AVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAY-----YHsgglrvnPNLYVDGKVCLSLLntwtgrg 929
Cdd:cd23794     22 EFPDPNDLLKfEVTITPDEGYYKGGTFVFEIDIPDNYPFEPPKVKcltkiYH-------PNIDEEGNVCLNIL------- 87

                           90       100
                   ....*....|....*....|....
gi 1002233178  930 NEVWDPsSSSILQVLVSLQGLVLN 953
Cdd:cd23794     88 REDWKP-VLSLKDVILGLLFLFLE 110

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  840 EWNILEKNLPDYIYVRVFEDRMDLIR--AVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAYY-----HsgglrvnPNL- 911
Cdd:cd23812      6 ELRELQKEPNDPDIVLGPVEDDDLFRweAVIKGPKDTPYEGGRFELAIQVPSNYPISPPKVKFvtkifH-------PNVh 78

                           90
                   ....*....|....*.
gi 1002233178  912 YVDGKVCLSLLNT-WT 926
Cdd:cd23812     79 FKTGEICLDILKTaWS 94

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).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233178  852 IYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAY-----YHsgglrvnPNL-YVDGKVCLSLLNTw 925
Cdd:cd23800     21 IKVELVGDDLTHLKGEIAGPPDTPYEGGTFVLDIKIPDTYPFEPPKMKfitkiWH-------PNIsSQTGAICLDILKD- 92

                           90       100
                   ....*....|....*....|....*
gi 1002233178  926 tgrgneVWDPsSSSILQVLVSLQGL 950
Cdd:cd23800     93 ------QWSP-ALTLRTALLSIQAL 110

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 1002233178  835 KKVQQEWNILEKNLPDYIYVRVFEDRMDLIRAVIIGASGTPYQDGLFFFDFHLPPEFPQVPPSAY-----YHsgglrvnP 909
Cdd:cd23801      3 RRLQKELEELRKSGPKYFRDLSVDESNVLKWTGLLVPDNPPYNKGAFRIEITFPAEYPFKPPKITfktkiYH-------P 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1002233178  910 NLYVDGKVCLSLLNTwtgrgnEVWDPsSSSILQVLVSLQGLVLNEKP 956
Cdd:cd23801     76 NVDEKGQVCLPIISP------ENWKP-ATKIDQVLQALLALINDPEP 115

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002233178  875 PYQDGLFFFDFHLPPEFPQVPPSAYYHSGGL--RVNPnlyVDGKVCLSLLNTwtgrgneVWDPSSSSILQVLVSLQ 948
Cdd:cd23814     40 LYKGGIFRFTISIPDNYPDGPPRVTFLSPVFhpLVDP---QTGELDLSRAFP-------KWRPGKHHIWHVLNYLK 105

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 1002233178  874 TPYQDGLFFFDFHLPPEFPQVPPS-----AYYHsgglrvnPNLYVDGKVCLSLLNTwTGR-------GNEVWDPSSS--S 939
Cdd:cd23811     44 SIYNGGYFKAEMVFPRDYPFSPPSfrflpPIFH-------PNVYPDGRLCISILHS-PGDdyqsgepAAERWSPAQTveS 115

                   ....*...
gi 1002233178  940 ILQVLVSL 947
Cdd:cd23811    116 VLLSILSL 123