U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.

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                  ....*....|....*....|....*....|....*....|....*....|..
gi 2186501638 481 SRLVCFISGEPMNENNQPLMLPNGYVYGEKSLRKMADDNDGKVTCPRTNESF 532
Cdd:cd16659     1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEKNDGKVVCPRTGESF 52

U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2186501638 481 SRLVCFISGEPMNENNQPLMLPNGYVYGEKSLRKMADDNDGKVTCPRTNESF 532
Cdd:cd16659     1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEKNDGKVVCPRTGESF 52

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.

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                   ....*....|....*....|....*....|....*....|....*...
gi 2186501638  483 LVCFISGEPMNEnnqPLMLPNGYVYGEKSLRKMADDNDgkvTCPRTNE 530
Cdd:smart00504   2 FLCPISLEVMKD---PVILPSGQTYERSAIEKWLLSHG---TDPVTGQ 43

U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2186501638 481 SRLVCFISGEPMNENNQPLMLPNGYVYGEKSLRKMADDNDGKVTCPRTNESF 532
Cdd:cd16659     1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEKNDGKVVCPRTGESF 52

C-terminal to LisH motif; Alpha-helical motif of unknown function.

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                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2186501638  297 TNIDIFLVCKDIElslaKHETSRCLSWCHENKSKLRKIKSTLEFSLRQQEFIELIRSEQRVE 358
Cdd:smart00668   1 EFDERKRIRELIL----KGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.

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                  ....*....|....*....|....*....|....*....|....*....
gi 2186501638 483 LVCFISGEPMNEnnqPLMLPNGYVYGEKSLRK-MADDNdgkvTCPRTNE 530
Cdd:cd16453     1 FLCPISGELMKD---PVITPSGITYDRSAIERwLLSDN----TDPFTRE 42