F-box protein 5 [Homo sapiens]
Protein Classification
F-box only protein 5( domain architecture ID 17779917)
F-box only protein 5 functions as a regulator of APC activity during mitotic and meiotic cell cycle; during mitotic cell cycle, it plays a role as both substrate and inhibitor of the APC-FZR1 complex
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 ... |
369-425 | 2.78e-27 | ||
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: 103.33 E-value: 2.78e-27
|
||||||
| F-box_FBXO5 | cd22170 | F-box domain found in F-box only protein 5 (FBXO5) and similar proteins; FBXO5, also called ... |
248-296 | 7.43e-22 | ||
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: 88.25 E-value: 7.43e-22
|
||||||
| 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 ... |
369-425 | 2.78e-27 | ||
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: 103.33 E-value: 2.78e-27
|
||||||
| F-box_FBXO5 | cd22170 | F-box domain found in F-box only protein 5 (FBXO5) and similar proteins; FBXO5, also called ... |
248-296 | 7.43e-22 | ||
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: 88.25 E-value: 7.43e-22
|
||||||
| F-box | pfam00646 | F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ... |
257-289 | 5.36e-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: 34.82 E-value: 5.36e-03
|
||||||
| 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 ... |
369-425 | 2.78e-27 | ||
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: 103.33 E-value: 2.78e-27
|
||||||
| F-box_FBXO5 | cd22170 | F-box domain found in F-box only protein 5 (FBXO5) and similar proteins; FBXO5, also called ... |
248-296 | 7.43e-22 | ||
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: 88.25 E-value: 7.43e-22
|
||||||
| BRcat_RBR_EMI | cd20348 | BRcat domain found in early mitotic inhibitor (EMI) subfamily of F-box proteins; The EMI ... |
372-420 | 5.70e-19 | ||
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: 80.09 E-value: 5.70e-19
|
||||||
| BRcat_RBR_FBXO43 | cd20365 | BRcat domain found in F-box only protein 43 (FBXO43); FBXO43, also called FBX43 or endogenous ... |
372-422 | 1.15e-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: 70.59 E-value: 1.15e-15
|
||||||
| F-box_EMI | cd22086 | F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI ... |
248-295 | 8.25e-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: 62.51 E-value: 8.25e-13
|
||||||
| F-box_FBXO43 | cd22171 | F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called ... |
248-293 | 2.06e-06 | ||
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: 44.39 E-value: 2.06e-06
|
||||||
| F-box | pfam00646 | F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ... |
257-289 | 5.36e-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: 34.82 E-value: 5.36e-03
|
||||||
| Blast search parameters | ||||
|
