ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and similar proteins; This family represents a group of ubiquitin-like (Ubl) domain-containing proteins evolutionarily conserved and found in metazoa, fungi, and plants. They may regulate the activity and/or specificity of E2 ubiquitin conjugating enzymes belonging to the UBE2D family. Members in this family contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356941 163 LKLRISsTMTDVKLPVYSKDTVGQCKKKLQAAEGVDACCQRWFYSGKLLGDKVPIDECSIHQGYVVQVIV 232
Cdd:cd01794   1 LKLRLS-TGKDLKLSVRSTDTVLQAKRRLQALEGIEPSRQRWFFSGKLLTDKTRIEDAKIPKGFVVQVIV 69

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and similar proteins; This family represents a group of ubiquitin-like (Ubl) domain-containing proteins evolutionarily conserved and found in metazoa, fungi, and plants. They may regulate the activity and/or specificity of E2 ubiquitin conjugating enzymes belonging to the UBE2D family. Members in this family contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356941 163 LKLRISsTMTDVKLPVYSKDTVGQCKKKLQAAEGVDACCQRWFYSGKLLGDKVPIDECSIHQGYVVQVIV 232
Cdd:cd01794   1 LKLRLS-TGKDLKLSVRSTDTVLQAKRRLQALEGIEPSRQRWFFSGKLLTDKTRIEDAKIPKGFVVQVIV 69

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

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                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356941   174 VKLPVYSKDTVGQCKKKLQAAEGVDAC---CQRWFYSGKLLGDKVPIDECSIHQGYVVQVIV 232
Cdd:TIGR00601  13 FKIDMEPDETVKELKEKIEAEQGKDAYpvaQQKLIYSGKILSDDKTVKEYKIKEKDFVVVMV 74

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and similar proteins; This family represents a group of ubiquitin-like (Ubl) domain-containing proteins evolutionarily conserved and found in metazoa, fungi, and plants. They may regulate the activity and/or specificity of E2 ubiquitin conjugating enzymes belonging to the UBE2D family. Members in this family contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356941 163 LKLRISsTMTDVKLPVYSKDTVGQCKKKLQAAEGVDACCQRWFYSGKLLGDKVPIDECSIHQGYVVQVIV 232
Cdd:cd01794   1 LKLRLS-TGKDLKLSVRSTDTVLQAKRRLQALEGIEPSRQRWFFSGKLLTDKTRIEDAKIPKGFVVQVIV 69

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein 2 (UBTD2); UBTD2, also termed dendritic cell-derived ubiquitin-like protein (DC-UbP), or ubiquitin-like protein SB72, is a potential ubiquitin shuttle protein firstly identified in dendritic cells and implicated in apoptosis. It binds proteins involved in the ubiquitination pathway and may play an important role in regulating protein ubiquitination and delivery of ubiquitinated substrates in eukaryotic cells. UBTD2 is expressed in tumor cells but not in normal human adult tissue suggesting a role in tumorogenesis. It can potentially regulate the stability of proteins involved in various physiological processes relevant to many disease phenotypes, such as ageing and cancer. UBTD2 reconciles protein ubiquitination and deubiquitination via linking UbE1 and USP5 enzymes.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356941 163 LKLRISsTMTDVKLPVYSKDTVGQCKKKLQAAEGVDACCQRWFYSGKLLGDKVPIDECSIHQGYVVQVIVN 233
Cdd:cd17121   4 LRLRLS-TGKDLKLAVRSTDTVYHMKRRLHTAEGVEPGSQRWFFSGRPLTDKMKLEELKIPKDYVVQVIVS 73

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356941 161 IFLKLRISSTMTdvkLPVYSKDTVGQCKKKLQAAEGVDACCQRWFYSGKLLGDKVPIDECSIHQGYVVQVI 231
Cdd:cd17039   1 ITVKTLDGKTYT---VEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68

ubiquitin-like (Ubl) domain found in the Rad23 protein family; 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 an ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. The Ubl domain is responsible for the binding to proteasome. The UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates, which suggests Rad23 proteins might be involved in certain pathways of Ub metabolism. Both the Ubl domain and the XPC-binding domain are necessary for efficient NER function of Rad23 proteins.

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                ....*....|....*....|....*....|....*....|....*....
gi 21356941 182 DTVGQCKKKLQAAEGV-DACCQRWFYSGKLLGDKVPIDECSI-HQGYVV 228
Cdd:cd01805  21 DTVLELKEKIEQEQGDfPASGQKLIYSGKVLKDDKTLSEYNIkEKDFVV 69

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression

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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356941    161 IFLKLRISSTMTdVKLPVYSKDTVGQCKKKLQAAEGVDACCQRWFYSGKLLGDKVPIDECSIHQGYVVQVIV 232
Cdd:smart00213   1 IELTVKTLDGKT-ITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVL 71

ubiquitin-like (Ubl) domain 2 found in interferon-stimulated gene 15 (ISG15) and similar proteins; ISG15, also termed interferon-induced 15 kDa protein, or interferon-induced 17 kDa protein (IP17), or ubiquitin cross-reactive protein (UCRP), is an antiviral interferon-induced ubiquitin-like protein that upon viral infection it modifies cellular and viral proteins by mechanisms similar to ubiquitination. Although ISG15 has properties similar to those of other ubiquitin-like (Ubl) molecules, it is a unique member of the Ubl superfamily, whose expression and conjugation to target proteins are tightly regulated by specific signaling pathways, indicating it may have specialized functions in the immune system. ISG15 contains two tandem Ubl domains with a beta-grasp Ubl fold. This family corresponds to the second Ubl domain.

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                ....*....|....*....|....*....|....*....|....*....|..
gi 21356941 178 VYSKDTVGQCKKKLQAAEGVDACCQRWFYSGKLLGDKVPIDE------CSIH 223
Cdd:cd01810  17 VRLTQTVDQLKQKVSGREGVHDDQFWLTFEGRPLEDQLPLGEyglkpqSTIH 68