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Conserved domains on  [gi|81894676|sp|Q7TSG3|]
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RecName: Full=F-box only protein 5; AltName: Full=Early mitotic inhibitor 1

Protein Classification

Graphical summary

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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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81894676 343 LKNNESLKACVRCNFPAKYDHYLERAVCKRESCQFEYCTKCLCAYHNNKDCLNGKIL 399
Cdd:cd20364   1 LKNDESLKACVRCNSPAKYDPYLQRATCTRESCGFDFCTKCLCKYHGSKDCLNGKPL 57
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
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 81894676 223 AELSRRGFVHLLANILTKLSGMDLVNLSKVSRIWKKILENNKGAFQLYS 271
Cdd:cd22170   1 AELFLRDLKHVLAKILRHLSDMDLINCSKVSTTWRKILQEDKWAFQIYS 49
 
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81894676 343 LKNNESLKACVRCNFPAKYDHYLERAVCKRESCQFEYCTKCLCAYHNNKDCLNGKIL 399
Cdd:cd20364   1 LKNDESLKACVRCNSPAKYDPYLQRATCTRESCGFDFCTKCLCKYHGSKDCLNGKPL 57
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
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 81894676 223 AELSRRGFVHLLANILTKLSGMDLVNLSKVSRIWKKILENNKGAFQLYS 271
Cdd:cd22170   1 AELFLRDLKHVLAKILRHLSDMDLINCSKVSTTWRKILQEDKWAFQIYS 49
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
                           10        20        30
                   ....*....|....*....|....*....|...
gi 81894676    232 HLLANILTKLSGMDLVNLSKVSRIWKKILENNK 264
Cdd:smart00256   4 EILEEILSKLDPKDLLRLRKVSRKWRSLIDSHD 36
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 81894676   232 HLLANILTKLSGMDLVNLSKVSRIWKKILENNK 264
Cdd:pfam00646   7 DLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLK 39
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 81894676   341 KTLKNNESLKACVR--CNFPAKYDH---YLERAVCKreSCQFEYCTKCLCAYHNNKDC 393
Cdd:pfam01485  10 SYVESDPNLKWCPTpdCGYIIELTDgcsNTSHVTCS--KCGHEFCFNCKEEWHEGLTC 65
 
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81894676 343 LKNNESLKACVRCNFPAKYDHYLERAVCKRESCQFEYCTKCLCAYHNNKDCLNGKIL 399
Cdd:cd20364   1 LKNDESLKACVRCNSPAKYDPYLQRATCTRESCGFDFCTKCLCKYHGSKDCLNGKPL 57
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
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 81894676 346 NESLKACVRCNFPAKYDHYLERAVCKRESCQFEYCTKCLCAYHNNKDC 393
Cdd:cd20348   1 GESLRPCPRCSSPAKVDPVEQRATCTRETCGFDFCTKCLCEFHGSKPC 48
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
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 81894676 223 AELSRRGFVHLLANILTKLSGMDLVNLSKVSRIWKKILENNKGAFQLYS 271
Cdd:cd22170   1 AELFLRDLKHVLAKILRHLSDMDLINCSKVSTTWRKILQEDKWAFQIYS 49
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 81894676 346 NESLKACVRCNFPAKYDHYLERAVCKRESCQFEYCTKCLCAYHNNKDCLNG 396
Cdd:cd20365   1 DEALKPCPRCQSPAKYQPVKKRGLCSREACGFDFCVLCLCAFHGSKECTSG 51
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
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 81894676 224 ELSRRGFVHLLANILTKLSGMDLVNLSKVSRIWKKILENNKGAFQLY 270
Cdd:cd22086   2 ELHKRNCPHILSKILSYLSPEDLCRVSCVSKTWRQICLSDPKANRRR 48
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
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 81894676 223 AELSRRGFVHLLANILTKLSGMDLVNLSKVSRIWKKILENNKGAFQ 268
Cdd:cd22171   1 AELKNRNLKHILAIILDLLTAESICSFWKVSKNWRDIIVQDKSAYQ 46
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
                           10        20        30
                   ....*....|....*....|....*....|...
gi 81894676    232 HLLANILTKLSGMDLVNLSKVSRIWKKILENNK 264
Cdd:smart00256   4 EILEEILSKLDPKDLLRLRKVSRKWRSLIDSHD 36
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 81894676   232 HLLANILTKLSGMDLVNLSKVSRIWKKILENNK 264
Cdd:pfam00646   7 DLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLK 39
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 81894676   341 KTLKNNESLKACVR--CNFPAKYDH---YLERAVCKreSCQFEYCTKCLCAYHNNKDC 393
Cdd:pfam01485  10 SYVESDPNLKWCPTpdCGYIIELTDgcsNTSHVTCS--KCGHEFCFNCKEEWHEGLTC 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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