PREDICTED: F-box only protein 43 [Propithecus coquereli]
Protein Classification
F-box only protein 43( domain architecture ID 17779923)
F-box only protein 43 that is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization; acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| BRcat_RBR_FBXO43 | cd20365 | BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous ... |
629-678 | 1.55e-32 | ||
BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous meiotic inhibitor 2 (EMI2), plays a key role during the meiotic cell cycle. It is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. It probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. It may recognize and bind to some phosphorylated proteins and promotes their ubiquitination and degradation. FBXO43 contains an F-box domain, and the first half of the RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the BRcat (benign-catalytic) domain that adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. : Pssm-ID: 439026 Cd Length: 51 Bit Score: 119.52 E-value: 1.55e-32
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| F-box_FBXO43 | cd22171 | F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called ... |
494-542 | 3.38e-24 | ||
F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called FBX43, or endogenous meiotic inhibitor 2 (EMI2), plays a key role during the meiotic cell cycle. It is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. It probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. It may recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. : Pssm-ID: 438942 Cd Length: 49 Bit Score: 95.62 E-value: 3.38e-24
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| Name | Accession | Description | Interval | E-value | ||
| BRcat_RBR_FBXO43 | cd20365 | BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous ... |
629-678 | 1.55e-32 | ||
BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous meiotic inhibitor 2 (EMI2), plays a key role during the meiotic cell cycle. It is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. It probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. It may recognize and bind to some phosphorylated proteins and promotes their ubiquitination and degradation. FBXO43 contains an F-box domain, and the first half of the RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the BRcat (benign-catalytic) domain that adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. Pssm-ID: 439026 Cd Length: 51 Bit Score: 119.52 E-value: 1.55e-32
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| F-box_FBXO43 | cd22171 | F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called ... |
494-542 | 3.38e-24 | ||
F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called FBX43, or endogenous meiotic inhibitor 2 (EMI2), plays a key role during the meiotic cell cycle. It is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. It probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. It may recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. Pssm-ID: 438942 Cd Length: 49 Bit Score: 95.62 E-value: 3.38e-24
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| IBR | pfam01485 | IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found ... |
617-676 | 5.65e-05 | ||
IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers (pfam00097). This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought to exist in all eukaryotic organizms. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes. The ubiquitin ligase Parkin is an RBR family protein whose mutations are involved in forms of familial Parkinson's disease. Pssm-ID: 460227 Cd Length: 65 Bit Score: 41.38 E-value: 5.65e-05
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| IBR | smart00647 | In Between Ring fingers; the domains occurs between pairs og RING fingers |
632-676 | 7.56e-04 | ||
In Between Ring fingers; the domains occurs between pairs og RING fingers Pssm-ID: 214763 [Multi-domain] Cd Length: 64 Bit Score: 38.16 E-value: 7.56e-04
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| FBOX | smart00256 | A Receptor for Ubiquitination Targets; |
503-542 | 3.36e-03 | ||
A Receptor for Ubiquitination Targets; Pssm-ID: 197608 Cd Length: 41 Bit Score: 35.88 E-value: 3.36e-03
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| Name | Accession | Description | Interval | E-value | ||
| BRcat_RBR_FBXO43 | cd20365 | BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous ... |
629-678 | 1.55e-32 | ||
BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous meiotic inhibitor 2 (EMI2), plays a key role during the meiotic cell cycle. It is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. It probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. It may recognize and bind to some phosphorylated proteins and promotes their ubiquitination and degradation. FBXO43 contains an F-box domain, and the first half of the RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the BRcat (benign-catalytic) domain that adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. Pssm-ID: 439026 Cd Length: 51 Bit Score: 119.52 E-value: 1.55e-32
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| F-box_FBXO43 | cd22171 | F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called ... |
494-542 | 3.38e-24 | ||
F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called FBX43, or endogenous meiotic inhibitor 2 (EMI2), plays a key role during the meiotic cell cycle. It is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. It probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. It may recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. Pssm-ID: 438942 Cd Length: 49 Bit Score: 95.62 E-value: 3.38e-24
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| BRcat_RBR_EMI | cd20348 | BRcat domain found in early mitotic inhibitor (EMI) subfamily of F-box proteins; The EMI ... |
629-677 | 1.44e-23 | ||
BRcat domain found in early mitotic inhibitor (EMI) subfamily of F-box proteins; The EMI subfamily includes FBXO5 (EMI1) and FBXO43 (EMI2), which are anaphase-promoting-complex/cyclosome (APC/C) inhibitors that bind APC/C-CCD20 (Cell division cycle protein 20) and/or APC/C-CDH1 (CDC20 homolog 1) complexes. FBXO5, also called FBX5, or early mitotic inhibitor 1 (EMI1), acts as a regulator that inhibits the anaphase-promoting complex/cyclosome (APC/C), which controls cell cycle progression through the sequential degradation of various substrates from S phase to early mitosis. During the mitotic cell cycle, it plays a role as both substrate and inhibitor of the APC-FZR1 complex. During G1 phase, it plays a role as substrate of the APC-FZR1 complex E3 ligase. FBXO43, also called FBX43, or endogenous meiotic inhibitor 2 (EMI2), plays a key role during the meiotic cell cycle. It is required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. It probably acts by inhibiting the APC/C ubiquitin ligase. It may recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Both FBXO5 and FBXO43 contain an F-box domain, and the first half of the RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the BRcat domain of the EMI subfamily that adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. Pssm-ID: 439009 Cd Length: 51 Bit Score: 93.96 E-value: 1.44e-23
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| BRcat_RBR_FBXO5 | cd20364 | BRcat domain found in F-box only protein 5 (FBXO5); FBXO5, also called FBX5 or early mitotic ... |
629-677 | 1.10e-17 | ||
BRcat domain found in F-box only protein 5 (FBXO5); FBXO5, also called FBX5 or early mitotic inhibitor 1 (EMI1), acts as a regulator that inhibits the anaphase-promoting complex/cyclosome (APC/C), which controls cell cycle progression through the sequential degradation of various substrates from S phase to early mitosis. During mitotic cell cycle, it plays a role as both substrate and inhibitor of the APC-FZR1 complex. During G1 phase, it plays a role as substrate of the APC-FZR1 complex E3 ligase. FBXO5 contains an F-box domain, and the first half of the RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the BRcat domain of FBXO5 that adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. Pssm-ID: 439025 Cd Length: 57 Bit Score: 77.14 E-value: 1.10e-17
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| F-box_EMI | cd22086 | F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI ... |
494-541 | 1.46e-13 | ||
F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI family includes FBX5 (EMI1) and FBX43 (EMI2), which are anaphase-promoting complex/cyclosome (APC/C) inhibitors that bind APC/C-CCD20 (Cell division cycle protein 20) and/or APC/C-CDH1 (CDC20 homologue 1) complexes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. Pssm-ID: 438858 Cd Length: 48 Bit Score: 65.21 E-value: 1.46e-13
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| BRcat_RBR_RNF14 | cd20341 | BRcat domain found in RING finger protein 14 (RNF14); RNF14, also called androgen receptor (AR) ... |
635-676 | 6.27e-08 | ||
BRcat domain found in RING finger protein 14 (RNF14); RNF14, also called androgen receptor (AR)-associated protein 54 (ARA54), HFB30, or Triad2 protein, is an RBR-type E3 ubiquitin-protein ligase that is highly expressed in the testis and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3). Its differential localization may play an important role in testicular development and spermatogenesis in humans. RNF14 functions as a transcriptional regulator of mitochondrial and immune function in muscles. It is a ligand-dependent AR co-activator that enhances AR-dependent transcriptional activation. It may also participate in enhancing cell cycle progression and cell proliferation via induction of cyclin D1. Moreover, RNF14 is crucial for colon cancer cell survival. It acts as a new enhancer of the Wnt-dependent transcriptional outputs that acts at the level of the T-cell factor/lymphoid enhancer factor (TCF/LEF)-beta-catenin complex. RNF14 contains an N-terminal RWD domain, and a C-terminal RBR domain. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the BRcat domain of RNF14 that adopts the same fold as the Rcat domain while lacking the catalytic cysteine residue and ubiquitination activity. Pssm-ID: 439002 Cd Length: 57 Bit Score: 49.61 E-value: 6.27e-08
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| F-box_FBXO5 | cd22170 | F-box domain found in F-box only protein 5 (FBXO5) and similar proteins; FBXO5, also called ... |
495-537 | 2.04e-07 | ||
F-box domain found in F-box only protein 5 (FBXO5) and similar proteins; FBXO5, also called FBX5, or early mitotic inhibitor 1 (EMI1), acts as a regulator that inhibits the anaphase-promoting complex/cyclosome (APC/C), which controls cell cycle progression through the sequential degradation of various substrates from S phase to early mitosis. During mitotic cell cycle, it plays a role as both substrate and inhibitor of the APC-FZR1 complex. During G1 phase, it plays a role as substrate of the APC-FZR1 complex E3 ligase. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. Pssm-ID: 438941 Cd Length: 49 Bit Score: 47.80 E-value: 2.04e-07
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| Rcat_RBR_parkin | cd20357 | Rcat domain found in parkin and similar proteins; Parkin, also called Parkinson juvenile ... |
628-676 | 5.81e-06 | ||
Rcat domain found in parkin and similar proteins; Parkin, also called Parkinson juvenile disease protein 2, is an RBR-type E3 ubiquitin-protein ligase that is associated with recessive early onset Parkinson's disease (PD), and exerts a protective effect against dopamine-induced alpha-synuclein-dependent cell toxicity. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Parkin functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746, and AIMP2. It mediates monoubiquitination as well as Lys6-, Lys11-, Lys48- and Lys63-linked polyubiquitination of substrates depending on the context. Parkin may enhance cell viability and protects dopaminergic neurons from oxidative stress-mediated death by regulating mitochondrial function. It also limits the production of reactive oxygen species (ROS), and regulates cyclin-E during neuronal apoptosis. Moreover, parkin displays a ubiquitin ligase-independent function in transcriptional repression of p53. Parkin contains an N-terminal ubiquitin-like domain and a C-terminal RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain of parkin that is essential for RBR E3 ligase activity and adopts the same fold as the BRcat domain. Pssm-ID: 439018 Cd Length: 55 Bit Score: 43.92 E-value: 5.81e-06
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| IBR | pfam01485 | IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found ... |
617-676 | 5.65e-05 | ||
IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers (pfam00097). This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought to exist in all eukaryotic organizms. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes. The ubiquitin ligase Parkin is an RBR family protein whose mutations are involved in forms of familial Parkinson's disease. Pssm-ID: 460227 Cd Length: 65 Bit Score: 41.38 E-value: 5.65e-05
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| Rcat_RBR_HHARI-like | cd20356 | Rcat domain found in human homolog of Drosophila Ariadne (HHARI) and similar proteins; This ... |
633-678 | 4.13e-04 | ||
Rcat domain found in human homolog of Drosophila Ariadne (HHARI) and similar proteins; This subfamily includes Drosophila melanogaster protein ariadne-1 (ARI-1), and its eukaryotic homologs, such as HHARI. ARI-1 is a widely expressed Drosophila RING-finger protein that localizes mainly in the cytoplasm, and is required for neural development. It interacts with the ubiquitin-conjugating enzyme, UbcD10. HHARI is also called H7-AP2, monocyte protein 6 (MOP-6), protein ariadne-1 homolog, Ariadne RBR E3 ubiquitin protein ligase 1 (ARIH1), ariadne-1 (ARI-1), UbcH7-binding protein, UbcM4-interacting protein, or ubiquitin-conjugating enzyme E2-binding protein. It is an RBR-type E3 ubiquitin-protein ligase highly expressed in nuclei, where it is co-localized with nuclear bodies including Cajal, PML, and Lewy bodies. It interacts with the E2 conjugating enzymes UbcH7, UbcH8, UbcM4 and UbcD10 in human, mouse and fly, and modulates the ubiquitylation of substrate proteins including single-minded 2 (SIM2) and translation initiation factor 4E homologous protein (4EHP). It functions as a potent mediator of DNA damage-induced translation arrest, which protects stem and cancer cells against genotoxic stress by initiating a 4EHP-mediated mRNA translation arrest. HHARI contains an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain of HHARI and similar proteins that are essential for RBR E3 ligase activity and adopts the same fold as the BRcat domain. Pssm-ID: 439017 Cd Length: 58 Bit Score: 38.88 E-value: 4.13e-04
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| Rcat_RBR_ARI7-like | cd22583 | Rcat domain found in E3 ubiquitin-protein ligase ARI7 and similar proteins; This subfamily ... |
633-678 | 5.39e-04 | ||
Rcat domain found in E3 ubiquitin-protein ligase ARI7 and similar proteins; This subfamily contains probable RBR-type E3 ubiquitin-protein ligases (EC 2.3.2.31) including Arabidopsis thaliana ARI5, ARI6, ARI7, and ARI8, as well as Dictyostelium discoideum RbrA (also called Ariadne-like ubiquitin ligase). They may function as part of E3 complexes, which accept ubiquitin from E2 ubiquitin-conjugating enzymes and then transfer it to substrates. RbrA may be required for normal cell-type proportioning and cell sorting during multicellular development, and is also necessary for spore cell viability. Members of this subfamily contain an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain of ARI7-like proteins that are essential for RBR E3 ligase activity and adopt the same fold as the BRcat domain. Pssm-ID: 439034 Cd Length: 55 Bit Score: 38.59 E-value: 5.39e-04
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| IBR | smart00647 | In Between Ring fingers; the domains occurs between pairs og RING fingers |
632-676 | 7.56e-04 | ||
In Between Ring fingers; the domains occurs between pairs og RING fingers Pssm-ID: 214763 [Multi-domain] Cd Length: 64 Bit Score: 38.16 E-value: 7.56e-04
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| F-box_FBXW1B | cd22183 | F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; ... |
491-531 | 2.72e-03 | ||
F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; FBXW1B, also called F-box/WD repeat-containing protein 11 (FBXW11), F-box and WD repeats protein beta-TrCP2, or homologous to Slimb protein (HOS), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as IFNAR1, CEP68 and CDC25A, as well as phosphorylated CTNNB1, NFKBIA, PER1 and PER2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. Pssm-ID: 438954 Cd Length: 51 Bit Score: 36.42 E-value: 2.72e-03
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| Rcat_RBR_TRIAD1 | cd20360 | Rcat domain found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1); TRIAD1, ... |
633-678 | 3.20e-03 | ||
Rcat domain found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1); TRIAD1, also called ariadne-2 (ARI-2), protein ariadne-2 homolog, Ariadne RBR E3 ubiquitin protein ligase 2 (ARIH2), or UbcM4-interacting protein 48, is an RBR-type E3 ubiquitin-protein ligase that catalyzes the formation of polyubiquitin chains linked via lysine-48 as well as lysine-63 residues. Its auto-ubiquitylation can be catalyzed by the E2 conjugating enzyme UBCH7. TRIAD1 has been implicated in hematopoiesis, specifically in myelopoiesis, as well as in embryogenesis. It functions as a regulator of endosomal transport, and is required for the proper function of multivesicular bodies. It also acts as a novel ubiquitination target for proteasome-dependent degradation by murine double minute 2 (MDM2). As a proapoptotic protein, TRIAD1 promotes p53 activation, and inhibits MDM2-mediated p53 ubiquitination and degradation. Furthermore, TRIAD1 can inhibit the ubiquitination and proteasomal degradation of growth factor independence 1 (Gfi1), a transcriptional repressor essential for the function and development of many different hematopoietic lineages. TRIAD1 contains an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain of TRIAD1 that is essential for RBR E3 ligase activity and adopts the same fold as the BRcat domain. Pssm-ID: 439021 Cd Length: 56 Bit Score: 36.21 E-value: 3.20e-03
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| FBOX | smart00256 | A Receptor for Ubiquitination Targets; |
503-542 | 3.36e-03 | ||
A Receptor for Ubiquitination Targets; Pssm-ID: 197608 Cd Length: 41 Bit Score: 35.88 E-value: 3.36e-03
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| Rcat_RBR_DEAH12-like | cd22585 | Rcat domain of ATP-dependent RNA helicase DEAH12 and similar proteins; This group includes ... |
633-676 | 5.51e-03 | ||
Rcat domain of ATP-dependent RNA helicase DEAH12 and similar proteins; This group includes Arabidopsis thaliana ATP-dependent RNA helicases DEAH11 and DEAH12, which may be bifunctional proteins that function as DEAD-box RNA helicases (EC 3.6.4.13) and RBR-type E3 ubiquitin-protein ligases (EC 2.3.2.31). As RNA helicases, they may utilize the energy from ATP hydrolysis to unwind RNA (or DNA). DEAD-box RNA helicases participate in every aspect of RNA metabolism. As E3 ubiquitin-protein ligase, they may function as part of E3 complexes, which accept ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfer it to substrates. Other members of this group may not have an RNA helicase domain. All members contain an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction. This model corresponds to the Rcat domain that is essential for RBR E3 ligase activity and adopts the same fold as the BRcat domain. Pssm-ID: 439036 Cd Length: 52 Bit Score: 35.40 E-value: 5.51e-03
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