RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375887 192 RNALEYTPEVFAQVSMLYINMEINGHPVKAFVDSGAQMTIISPRLAEKTELKRFIDNRFIGEARGVGTGKILGRVHQVQV 271
Cdd:cd05479     1 QNAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1215375887 272 KIETQFIPCSFVVLDS-NVDLLLGLDMLKRHQACIDLEKNVLRI 314
Cdd:cd05479    81 KIGNLFLPCSFTVLEDdDVDFLIGLDMLKRHQCVIDLKENVLRI 124

UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar proteins; Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also called transporter regulator RS1 (RS1) which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLF 425
Cdd:cd14309     1 EEKIAQLMDLGFSREEAIQALEATNGNVELAASLLF 36

RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375887 192 RNALEYTPEVFAQVSMLYINMEINGHPVKAFVDSGAQMTIISPRLAEKTELKRFIDNRFIGEARGVGTGKILGRVHQVQV 271
Cdd:cd05479     1 QNAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1215375887 272 KIETQFIPCSFVVLDS-NVDLLLGLDMLKRHQACIDLEKNVLRI 314
Cdd:cd05479    81 KIGNLFLPCSFTVLEDdDVDFLIGLDMLKRHQCVIDLKENVLRI 124

ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215375887   1 MQLTVTNDVNGEVYgPLELSGDMMLMDLVALLEVDCAFESGKQQLYFNGKELKPDvEKTLEELGIGNDDLIVIR 74
Cdd:cd01796     1 MKLTVTTEDDDRLF-SLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDD-KKTLEALGLKDGDLLLLR 72

Predicted aspartyl protease [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375887 209 YINMEINGHPVKAFVDSGAQMTIISPRLAEKTELKrFIDNRFIGEAR---GVGTGKIlGRVHQVQV-KIETQFIPCSFVV 284
Cdd:COG3577    43 VVEGTINGQPVRFLVDTGASTVVLSESDARRLGLD-PEDLGRPVRVQtanGVVRAAR-VRLDSVRIgGITLRNVRAVVLP 120

                          90       100
                  ....*....|....*....|....*....
gi 1215375887 285 LDSNVDLLLGLDMLKRHQACIDLEKNVLR 313
Cdd:COG3577   121 GGELDDGLLGMSFLGRLDFEIDGDRLTLR 149

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1215375887 388 FPEKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLL 424
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37

RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375887 192 RNALEYTPEVFAQVSMLYINMEINGHPVKAFVDSGAQMTIISPRLAEKTELKRFIDNRFIGEARGVGTGKILGRVHQVQV 271
Cdd:cd05479     1 QNAMEHHPESFGKVPMLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDKRFQGIAKGVGTQKILGRIHLAQV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1215375887 272 KIETQFIPCSFVVLDS-NVDLLLGLDMLKRHQACIDLEKNVLRI 314
Cdd:cd05479    81 KIGNLFLPCSFTVLEDdDVDFLIGLDMLKRHQCVIDLKENVLRI 124

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375887 210 INMEINGHPVKAFVDSGAQMTIISPRLAEKTELKRFIDNRFIGEARGVGTGKI-LGRVHQVQV-KIETQFIPCSfVVLDS 287
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISEALAERLGLDRLVDAYPVTVRTANGTVRAaRVRLDSVKIgGIELRNVPAV-VLPGD 79

                          90
                  ....*....|...
gi 1215375887 288 NVDLLLGLDMLKR 300
Cdd:pfam13975  80 LDDVLLGMDFLKR 92

UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar proteins; Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also called transporter regulator RS1 (RS1) which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLF 425
Cdd:cd14309     1 EEKIAQLMDLGFSREEAIQALEATNGNVELAASLLF 36

Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375887 210 INMEINGHPVKAFVDSGAQMTIISPRLAEKTELKRfIDNRFIGEARGVGTGKILGRVHQVQVKI-ETQFIPCSFVVLDSN 288
Cdd:pfam13650   1 VPVTINGKPVRFLVDTGASGTVISPSLAERLGLKV-RGLAYTVRVSTAGGRVSAARVRLDSLRLgGLTLENVPALVLDLG 79

                          90
                  ....*....|
gi 1215375887 289 --VDLLLGLD 296
Cdd:pfam13650  80 dlIDGLLGMD 89

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1215375887  389 PEKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLF 425
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37

Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215375887 207 MLYINMEINGHPVKAFVDSGAQMTIISPRLAEktELKRFIDNRFIGEARGVGtgkilGRVHQVQVKIET------QFIPC 280
Cdd:cd05483     2 HFVVPVTINGQPVRFLLDTGASTTVISEELAE--RLGLPLTLGGKVTVQTAN-----GRVRAARVRLDSlqiggiTLRNV 74

                          90       100
                  ....*....|....*....|..
gi 1215375887 281 SFVVLDSN---VDLLLGLDMLK 299
Cdd:cd05483    75 PAVVLPGDalgVDGLLGMDFLR 96

UBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar proteins; The family includes some uncharacterized Ddi and similar proteins which show a high level of sequence similarity with yeast Ddi1. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in yeast. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell.

                          10        20        30
                  ....*....|....*....|....*....|
gi 1215375887 393 IKQLMDLGFSRQEVIQALVSTNGNAEFAAS 422
Cdd:cd14310     1 IQTLVNLGATREQAINLLNAAGGNVDLAAS 30

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1215375887 393 IKQLMDLGFSRQEVIQALVSTNGNAEFAASLLFQ 426
Cdd:cd14306     1 VAKLMELGFPEEDCIRALRACGGNVEEAANWLLE 34

UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar proteins; UBAC2, also called phosphoglycerate dehydrogenase-like protein 1, is a ubiquitin-associated domain (UBA)-domain containing protein encoded by gene UBAC2 (or PHGDHL1), a risk gene for Behcet's disease (BD). It may play an important role in the development of BD through its transcriptional modulation. Members in this family contain an N-terminal rhomboid-like domain and a C-terminal UBA domain.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLL 424
Cdd:cd14305     3 EEQVQQLVDMGFSREDVLEALRQSNNDVNAATNLL 37

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLL 424
Cdd:cd14387     1 EESIAILMSMGFPRNRAIEALKRTNNNLDRALDWL 35

UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1215375887 389 PEKtIKQLMDLGFSRQEVIQALVSTNGNAEFAASLL 424
Cdd:cd14291     2 EDK-LQQLMEMGFSEAEARLALRACNGNVERAVDYI 36

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVST-NGNAEFAASLLFQ 426
Cdd:cd14296     1 EEAVSQLMSMGFSENAAKRALYYTgNSSVEAAMNWLFE 38

UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA1 domain.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLF 425
Cdd:cd14280     3 EATINNIMSMGFEREQVVRALRAAFNNPDRAVEYLL 38

UBA domain found in casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor proteins family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-3. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating the activated tyrosine kinases and targeting them for degradation. Cbl proteins in this family consists of a highly conserved N-terminal half that includes a tyrosine-kinase-binding (TKB) domain and a RING finger domain, both of which are required for Cbl-mediated downregulation of RTKs, and a C-terminal half that includes a ubiquitin-associated (UBA) domain and other protein interaction motifs. The UBA domain contains leucine/isoleucine repeats and may play a role in dimerization of Cbl proteins. In addition, although both c-Cbl and Cbl-b have the C-terminal UBA domain, only the UBA domain from Cbl-b can bind ubiquitin.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLFQ 426
Cdd:cd14318     2 LSYIAKLVGEGYSKEDVIRALGIARNNVEMARDILRE 38

UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a modular protein containing Tudor domain, a DUF/OB-fold motif and a ubiquitin-associated (UBA) domain. It shows both nucleic acid- and methyl-binding properties and can interact with methylated RNA-binding proteins, such as fragile X mental retardation protein (FMRP) and DEAD/H box-3 (also known as DDX3X/Y, DBX/Y, HLP2 and DDX14) which is implicated in human genetic diseases. At this point, TDRD3 may play a central role in RNA processing regulatory pathways involving arginine methylation. TDRD3 localizes predominantly to the cytoplasm stress granules (SGs). The Tudor domain is essential and sufficient for its recruitment to SGs.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLF 425
Cdd:cd14282     3 EKALRHITEMGFSKEAARQALMDNNNNLEAALNFLL 38

UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and similar proteins; UBE2K, also called Huntingtin-interacting protein 2 (HIP-2), ubiquitin carrier protein, ubiquitin-conjugating enzyme E2-25 kDa (E2-25K), or ubiquitin-protein ligase, is a multi-ubiquitinating enzyme with the ability to synthesize Lys48-linked polyubiquitin chains which is involved in the ubiquitin (Ub)-dependent proteolytic pathway. It interacts with the frameshift mutant of ubiquitin B and functions as a crucial factor regulating amyloid-beta neurotoxicity. It has also been characterized as Huntingtin-interacting protein that modulates the neurotoxicity of Amyloid-beta (Abeta), the principal protein involved in Alzheimer's disease pathogenesis. Moreover, E2-25K increases aggregate the formation of expanded polyglutamine proteins and polyglutamine-induced cell death in the pathology of polyglutamine diseases. UbcD4, also called ubiquitin carrier protein, or ubiquitin-protein ligase, is encoded by Drosophila E2 gene which is only expressed in pole cells in embryos. It is a putative E2 enzyme homologous to the Huntingtin interacting protein-2 (HIP2) of human. UbcD4 specifically interacts with the polyubiquitin-binding subunit of the proteasome. This family also includes a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE). It shows a high level of sequence similarity with UBE2K and may also plays a role in the ubiquitin-mediated protein degradation pathway. All family members are class II E2 conjugating enzymes which contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1215375887 390 EKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLF 425
Cdd:cd14313     1 KKKVDKLVDMGFDRDEAIVALSSNNWNLERATEYLF 36