U-box domain-containing protein [Arabidopsis lyrata subsp. lyrata]
Protein Classification
U-box domain-containing protein( domain architecture ID 11616232)
U-box domain-containing protein contains a modified RING finger and functions as an E3 ubiquitin ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
12-64 | 3.56e-25 | ||
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain. : Pssm-ID: 438326 [Multi-domain] Cd Length: 53 Bit Score: 96.86 E-value: 3.56e-25
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| Name | Accession | Description | Interval | E-value | ||
| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
12-64 | 3.56e-25 | ||
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain. Pssm-ID: 438326 [Multi-domain] Cd Length: 53 Bit Score: 96.86 E-value: 3.56e-25
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
15-77 | 4.24e-19 | ||
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination. Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 80.74 E-value: 4.24e-19
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| U-box | pfam04564 | U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ... |
11-77 | 3.67e-15 | ||
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues. Pssm-ID: 398320 [Multi-domain] Cd Length: 73 Bit Score: 70.03 E-value: 3.67e-15
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| Name | Accession | Description | Interval | E-value | ||
| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
12-64 | 3.56e-25 | ||
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain. Pssm-ID: 438326 [Multi-domain] Cd Length: 53 Bit Score: 96.86 E-value: 3.56e-25
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
15-77 | 4.24e-19 | ||
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination. Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 80.74 E-value: 4.24e-19
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| RING-Ubox_WDSUB1-like | cd16655 | U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ... |
12-67 | 3.35e-15 | ||
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis. Pssm-ID: 438317 [Multi-domain] Cd Length: 55 Bit Score: 69.45 E-value: 3.35e-15
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| U-box | pfam04564 | U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ... |
11-77 | 3.67e-15 | ||
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues. Pssm-ID: 398320 [Multi-domain] Cd Length: 73 Bit Score: 70.03 E-value: 3.67e-15
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| RING-Ubox | cd16453 | U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ... |
15-59 | 3.57e-11 | ||
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. Pssm-ID: 438117 [Multi-domain] Cd Length: 44 Bit Score: 57.56 E-value: 3.57e-11
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| RING-Ubox_LubX-like_rpt2 | cd23150 | second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ... |
12-77 | 1.78e-09 | ||
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one. Pssm-ID: 438512 [Multi-domain] Cd Length: 69 Bit Score: 53.62 E-value: 1.78e-09
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| RING-Ubox_CHIP | cd16654 | U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ... |
11-77 | 1.97e-09 | ||
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase. Pssm-ID: 438316 [Multi-domain] Cd Length: 71 Bit Score: 53.73 E-value: 1.97e-09
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| RING-Ubox_LubX-like_rpt1 | cd23149 | first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ... |
15-70 | 1.15e-08 | ||
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one. Pssm-ID: 438511 [Multi-domain] Cd Length: 55 Bit Score: 50.95 E-value: 1.15e-08
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| SPL-RING_NSE2 | cd16651 | SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ... |
15-75 | 3.00e-07 | ||
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity. Pssm-ID: 438313 [Multi-domain] Cd Length: 67 Bit Score: 47.26 E-value: 3.00e-07
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| RING-HC_TRIM41-like_C-IV | cd16602 | RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ... |
17-67 | 1.98e-03 | ||
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of the TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain. Pssm-ID: 438264 [Multi-domain] Cd Length: 53 Bit Score: 36.06 E-value: 1.98e-03
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