F-box only protein 5 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| BRcat_RBR_FBXO5 | cd20364 | BRcat domain found in F-box only protein 5 (FBXO5); FBXO5, also called FBX5 or early mitotic ... |
343-399 | 6.24e-28 | ||
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: 104.87 E-value: 6.24e-28
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| F-box_SF super family | cl45894 | F-box domain superfamily; This short domain is commonly found at the N-terminus of various ... |
223-271 | 1.01e-15 | ||
F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. 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. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures. The actual alignment was detected with superfamily member cd22170: Pssm-ID: 459239 Cd Length: 49 Bit Score: 70.91 E-value: 1.01e-15
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| Name | Accession | Description | Interval | E-value | ||
| BRcat_RBR_FBXO5 | cd20364 | BRcat domain found in F-box only protein 5 (FBXO5); FBXO5, also called FBX5 or early mitotic ... |
343-399 | 6.24e-28 | ||
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: 104.87 E-value: 6.24e-28
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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 ... |
223-271 | 1.01e-15 | ||
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: 70.91 E-value: 1.01e-15
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| FBOX | smart00256 | A Receptor for Ubiquitination Targets; |
232-264 | 4.87e-04 | ||
A Receptor for Ubiquitination Targets; Pssm-ID: 197608 Cd Length: 41 Bit Score: 37.42 E-value: 4.87e-04
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| F-box | pfam00646 | F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ... |
232-264 | 1.15e-03 | ||
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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: 425796 Cd Length: 43 Bit Score: 36.36 E-value: 1.15e-03
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| IBR | pfam01485 | IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found ... |
341-393 | 6.41e-03 | ||
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: 35.22 E-value: 6.41e-03
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| Name | Accession | Description | Interval | E-value | ||
| BRcat_RBR_FBXO5 | cd20364 | BRcat domain found in F-box only protein 5 (FBXO5); FBXO5, also called FBX5 or early mitotic ... |
343-399 | 6.24e-28 | ||
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: 104.87 E-value: 6.24e-28
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| BRcat_RBR_EMI | cd20348 | BRcat domain found in early mitotic inhibitor (EMI) subfamily of F-box proteins; The EMI ... |
346-393 | 1.90e-16 | ||
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: 72.77 E-value: 1.90e-16
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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 ... |
223-271 | 1.01e-15 | ||
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: 70.91 E-value: 1.01e-15
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| BRcat_RBR_FBXO43 | cd20365 | BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous ... |
346-396 | 6.54e-15 | ||
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: 68.67 E-value: 6.54e-15
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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 ... |
224-270 | 8.35e-09 | ||
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: 50.96 E-value: 8.35e-09
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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 ... |
223-268 | 1.46e-04 | ||
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: 39.38 E-value: 1.46e-04
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| FBOX | smart00256 | A Receptor for Ubiquitination Targets; |
232-264 | 4.87e-04 | ||
A Receptor for Ubiquitination Targets; Pssm-ID: 197608 Cd Length: 41 Bit Score: 37.42 E-value: 4.87e-04
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| F-box | pfam00646 | F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ... |
232-264 | 1.15e-03 | ||
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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: 425796 Cd Length: 43 Bit Score: 36.36 E-value: 1.15e-03
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| IBR | pfam01485 | IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found ... |
341-393 | 6.41e-03 | ||
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: 35.22 E-value: 6.41e-03
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