ubiquitin-like protein 3 [Homo sapiens]
ubiquitin family protein( domain architecture ID 13018376)
ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Ubl_UBL3 | cd17048 | ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; ... |
10-91 | 7.56e-64 | |||
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; UBL3, also termed membrane-anchored ubiquitin-fold protein (MUB), or protein HCG-1, belongs to a newly described MUB protein family with structural homology with ubiquitin. MUB proteins have a beta-grasp ubiquitin-like (Ubl) domain with longer N- and C-termini and extended loops. The Ubl domain contains a C-terminal CAAX-box, a canonical motif for protein prenylation, which is modified through protein lipidation with a hydrophobic membrane anchor. The lipidation and membrane localization inhibit attachment of MUBs to target proteins. : Pssm-ID: 340568 Cd Length: 82 Bit Score: 188.36 E-value: 7.56e-64
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Name | Accession | Description | Interval | E-value | |||
Ubl_UBL3 | cd17048 | ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; ... |
10-91 | 7.56e-64 | |||
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; UBL3, also termed membrane-anchored ubiquitin-fold protein (MUB), or protein HCG-1, belongs to a newly described MUB protein family with structural homology with ubiquitin. MUB proteins have a beta-grasp ubiquitin-like (Ubl) domain with longer N- and C-termini and extended loops. The Ubl domain contains a C-terminal CAAX-box, a canonical motif for protein prenylation, which is modified through protein lipidation with a hydrophobic membrane anchor. The lipidation and membrane localization inhibit attachment of MUBs to target proteins. Pssm-ID: 340568 Cd Length: 82 Bit Score: 188.36 E-value: 7.56e-64
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Rad60-SLD_2 | pfam13881 | Ubiquitin-2 like Rad60 SUMO-like; |
8-114 | 1.33e-50 | |||
Ubiquitin-2 like Rad60 SUMO-like; Pssm-ID: 372780 Cd Length: 111 Bit Score: 155.93 E-value: 1.33e-50
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UBQ | smart00213 | Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
10-88 | 4.38e-04 | |||
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 36.08 E-value: 4.38e-04
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Name | Accession | Description | Interval | E-value | |||
Ubl_UBL3 | cd17048 | ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; ... |
10-91 | 7.56e-64 | |||
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; UBL3, also termed membrane-anchored ubiquitin-fold protein (MUB), or protein HCG-1, belongs to a newly described MUB protein family with structural homology with ubiquitin. MUB proteins have a beta-grasp ubiquitin-like (Ubl) domain with longer N- and C-termini and extended loops. The Ubl domain contains a C-terminal CAAX-box, a canonical motif for protein prenylation, which is modified through protein lipidation with a hydrophobic membrane anchor. The lipidation and membrane localization inhibit attachment of MUBs to target proteins. Pssm-ID: 340568 Cd Length: 82 Bit Score: 188.36 E-value: 7.56e-64
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Rad60-SLD_2 | pfam13881 | Ubiquitin-2 like Rad60 SUMO-like; |
8-114 | 1.33e-50 | |||
Ubiquitin-2 like Rad60 SUMO-like; Pssm-ID: 372780 Cd Length: 111 Bit Score: 155.93 E-value: 1.33e-50
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Ubl_MUBs_plant | cd01814 | ubiquitin-like (Ubl) domain found in plant membrane-anchored ubiquitin-fold proteins (MUBs); ... |
9-91 | 2.73e-09 | |||
ubiquitin-like (Ubl) domain found in plant membrane-anchored ubiquitin-fold proteins (MUBs); The plant MUBs belong to a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation. They may serve as docking site to facilitate the association of specific E2s to the plasma membrane. MUBs contain a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. Pssm-ID: 340512 Cd Length: 89 Bit Score: 50.07 E-value: 2.73e-09
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Ubl_ubiquitin_like | cd17039 | ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
12-89 | 1.20e-05 | |||
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. Pssm-ID: 340559 [Multi-domain] Cd Length: 68 Bit Score: 40.27 E-value: 1.20e-05
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ubiquitin | pfam00240 | Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
12-88 | 1.22e-04 | |||
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites. Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 37.54 E-value: 1.22e-04
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UBQ | smart00213 | Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
10-88 | 4.38e-04 | |||
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 36.08 E-value: 4.38e-04
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Ubiquitin_like_fold | cd00196 | Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ... |
12-81 | 1.18e-03 | |||
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. Pssm-ID: 340450 Cd Length: 68 Bit Score: 34.99 E-value: 1.18e-03
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Blast search parameters | ||||
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