Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar proteins; WDR48, also termed USP1-associated factor 1 (UAF1), or WD repeat endosomal protein, or p80, is required for the histone deubiquitination activity. It stimulates activity of ubiquitin-specific proteases USP1, USP12, and USP46.As potential tumor suppressor, WDR48 in complex with deubiquitinase USP12 suppresses Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1). WDR48 also functions as a novel interaction partner of E1 helicase from anogenital human papillomavirus (HPV) types, and plays an essential role in anogenital HPV DNA replication. WDR48 contains a WD40 domain and a ubiquitin-like domain that shows high sequence and structural similarity with RING finger- and WD40-associated ubiquitin-like (RAWUL) domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820503834   3 KFNKIPFYLQPHSSSGA--KTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTtsssnnekqgeqekeediAVLAEEK 80
Cdd:cd17041     1 EFPKISFFLQPHPSSGLppKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQD------------------ASNPEEK 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1820503834  81 IELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 115
Cdd:cd17041    63 LELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97

Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar proteins; WDR48, also termed USP1-associated factor 1 (UAF1), or WD repeat endosomal protein, or p80, is required for the histone deubiquitination activity. It stimulates activity of ubiquitin-specific proteases USP1, USP12, and USP46.As potential tumor suppressor, WDR48 in complex with deubiquitinase USP12 suppresses Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1). WDR48 also functions as a novel interaction partner of E1 helicase from anogenital human papillomavirus (HPV) types, and plays an essential role in anogenital HPV DNA replication. WDR48 contains a WD40 domain and a ubiquitin-like domain that shows high sequence and structural similarity with RING finger- and WD40-associated ubiquitin-like (RAWUL) domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820503834   3 KFNKIPFYLQPHSSSGA--KTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTtsssnnekqgeqekeediAVLAEEK 80
Cdd:cd17041     1 EFPKISFFLQPHPSSGLppKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQD------------------ASNPEEK 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1820503834  81 IELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 115
Cdd:cd17041    63 LELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97

Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar proteins; WDR48, also termed USP1-associated factor 1 (UAF1), or WD repeat endosomal protein, or p80, is required for the histone deubiquitination activity. It stimulates activity of ubiquitin-specific proteases USP1, USP12, and USP46.As potential tumor suppressor, WDR48 in complex with deubiquitinase USP12 suppresses Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1). WDR48 also functions as a novel interaction partner of E1 helicase from anogenital human papillomavirus (HPV) types, and plays an essential role in anogenital HPV DNA replication. WDR48 contains a WD40 domain and a ubiquitin-like domain that shows high sequence and structural similarity with RING finger- and WD40-associated ubiquitin-like (RAWUL) domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820503834   3 KFNKIPFYLQPHSSSGA--KTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTtsssnnekqgeqekeediAVLAEEK 80
Cdd:cd17041     1 EFPKISFFLQPHPSSGLppKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQD------------------ASNPEEK 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1820503834  81 IELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 115
Cdd:cd17041    63 LELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820503834  20 KTLKKDRLSASDMLQVRKVMEHVYEKIInldnesqttsssnnekqgeqekeediavLAEEKIELLCQDQVLDPNMDLRTv 99
Cdd:cd00196     6 PSLKKIVVAVPPSTTLRQVLEKVAKRIG----------------------------LPPDVIRLLFNGQVLDDLMTAKQ- 56

                          90
                  ....*....|....*.
gi 1820503834 100 khfiWKSGGDLTLHYR 115
Cdd:cd00196    57 ----VGLEPGEELHFV 68

RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, DRIP and similar proteins; structurally similar to a beta-grasp ubiquitin-like fold; The family includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies that can remodel chromatin such that epigenetic silencing of genes takes place, and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development in fruit flies. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which are involved in the maintenance of gene repression and target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins, have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger, and a RAWUL domain that might be responsible for interaction with Cbx members of the Polycomb repression complexes.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1820503834  77 AEEKIELLCQDQVLDPNMDLRTVKHFIW-KSGGDLTLHYR 115
Cdd:cd16102    48 SEQDLDILCRGELLGKEHTLKFIWRTRWrKQDGPLVLQYR 87