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Conserved domains on  [gi|296480493|tpg|DAA22608|]
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TPA: F-box protein 43-like [Bos taurus]

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

CATH:  1.20.1280.50
Gene Symbol:  FBXO43
Gene Ontology:  GO:0046872|GO:0016567
PubMed:  11178263|31898225
SCOP:  4001927

Graphical summary

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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 ...
 831-881 9.20e-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: 117.59  E-value: 9.20e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296480493 831 DEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRG 881
Cdd:cd20365    1 DEALKPCPRCQSPAKYQPVKKRGLCSREACGFDFCVLCLCAFHGSKECTSG 51
F-box_FBXO43 cd22171
F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called ...
 696-744 1.26e-25

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: 99.85  E-value: 1.26e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 296480493 696 TELKYRNLKHVLAMVLDSLTAESLCSVWKVSRNWREIIVQDKKANRRRK 744
Cdd:cd22171    1 AELKNRNLKHILAIILDLLTAESICSFWKVSKNWRDIIVQDKSAYQRRK 49
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 113-209 7.63e-05

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493 113 TSPPGTSARWARPPRGpqVGGSGDARCATPARPRPVGGVLGPARPPSASPAWGGSADRRAAWLKPPGRPLTSHPPTA--- 189
Cdd:PRK07764 369 DDERGLLARLERLERR--LGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSpag 446

                         90       100
                 ....*....|....*....|....
gi 296480493 190 ----PRAGDDRAAADPAWQSEKFP 209
Cdd:PRK07764 447 napaGGAPSPPPAAAPSAQPAPAP 470
 
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 ...
 831-881 9.20e-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: 117.59  E-value: 9.20e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296480493 831 DEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRG 881
Cdd:cd20365    1 DEALKPCPRCQSPAKYQPVKKRGLCSREACGFDFCVLCLCAFHGSKECTSG 51
F-box_FBXO43 cd22171
F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called ...
 696-744 1.26e-25

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: 99.85  E-value: 1.26e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 296480493 696 TELKYRNLKHVLAMVLDSLTAESLCSVWKVSRNWREIIVQDKKANRRRK 744
Cdd:cd22171    1 AELKNRNLKHILAIILDLLTAESICSFWKVSKNWRDIIVQDKSAYQRRK 49
IBR pfam01485
IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found ...
 819-878 6.32e-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: 41.76  E-value: 6.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296480493  819 EEYVKVAKTLFIDEA--LKPCPR--CQSPAKYQPYKKRGL---CSRtaCGFDFCVLCLCAYHGSEEC 878
Cdd:pfam01485   1 EKYEKLLLKSYVESDpnLKWCPTpdCGYIIELTDGCSNTShvtCSK--CGHEFCFNCKEEWHEGLTC 65
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 113-209 7.63e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493 113 TSPPGTSARWARPPRGpqVGGSGDARCATPARPRPVGGVLGPARPPSASPAWGGSADRRAAWLKPPGRPLTSHPPTA--- 189
Cdd:PRK07764 369 DDERGLLARLERLERR--LGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSpag 446

                         90       100
                 ....*....|....*....|....
gi 296480493 190 ----PRAGDDRAAADPAWQSEKFP 209
Cdd:PRK07764 447 napaGGAPSPPPAAAPSAQPAPAP 470
FBOX smart00256
A Receptor for Ubiquitination Targets;
705-744 8.60e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 37.80  E-value: 8.60e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 296480493   705 HVLAMVLDSLTAESLCSVWKVSRNWREIIvqDKKANRRRK 744
Cdd:smart00256   4 EILEEILSKLDPKDLLRLRKVSRKWRSLI--DSHDFWFKL 41
IBR smart00647
In Between Ring fingers; the domains occurs between pairs og RING fingers
 834-878 1.49e-03

In Between Ring fingers; the domains occurs between pairs og RING fingers


Pssm-ID: 214763 [Multi-domain]  Cd Length: 64  Bit Score: 37.78  E-value: 1.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 296480493   834 LKPCPR--CQSPAKYQ--PYKKRGLCSrtACGFDFCVLCLCAYHGSEEC 878
Cdd:smart00647  18 LKWCPApdCSAAIIVTeeEGCNRVTCP--KCGFSFCFRCKVPWHSPVSC 64
 
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 ...
 831-881 9.20e-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: 117.59  E-value: 9.20e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296480493 831 DEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRG 881
Cdd:cd20365    1 DEALKPCPRCQSPAKYQPVKKRGLCSREACGFDFCVLCLCAFHGSKECTSG 51
F-box_FBXO43 cd22171
F-box domain found in F-box only protein 43 (FBXO43) and similar proteins; FBXO43, also called ...
 696-744 1.26e-25

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: 99.85  E-value: 1.26e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 296480493 696 TELKYRNLKHVLAMVLDSLTAESLCSVWKVSRNWREIIVQDKKANRRRK 744
Cdd:cd22171    1 AELKNRNLKHILAIILDLLTAESICSFWKVSKNWRDIIVQDKSAYQRRK 49
BRcat_RBR_EMI cd20348
BRcat domain found in early mitotic inhibitor (EMI) subfamily of F-box proteins; The EMI ...
 831-879 8.57e-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: 92.03  E-value: 8.57e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 296480493 831 DEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECS 879
Cdd:cd20348    1 GESLRPCPRCSSPAKVDPVEQRATCTRETCGFDFCTKCLCEFHGSKPCP 49
BRcat_RBR_FBXO5 cd20364
BRcat domain found in F-box only protein 5 (FBXO5); FBXO5, also called FBX5 or early mitotic ...
 831-886 2.18e-18

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: 79.45  E-value: 2.18e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296480493 831 DEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRGaaKPR 886
Cdd:cd20364    4 DESLKACVRCNSPAKYDPYLQRATCTRESCGFDFCTKCLCKYHGSKDCLNG--KPL 57
F-box_EMI cd22086
F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI ...
 696-743 4.71e-14

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: 67.14  E-value: 4.71e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 296480493 696 TELKYRNLKHVLAMVLDSLTAESLCSVWKVSRNWREIIVQDKKANRRR 743
Cdd:cd22086    1 SELHKRNCPHILSKILSYLSPEDLCRVSCVSKTWRQICLSDPKANRRR 48
F-box_FBXO5 cd22170
F-box domain found in F-box only protein 5 (FBXO5) and similar proteins; FBXO5, also called ...
 697-739 7.51e-09

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: 52.42  E-value: 7.51e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 296480493 697 ELKYRNLKHVLAMVLDSLTAESLCSVWKVSRNWREIIVQDKKA 739
Cdd:cd22170    2 ELFLRDLKHVLAKILRHLSDMDLINCSKVSTTWRKILQEDKWA 44
BRcat_RBR_RNF14 cd20341
BRcat domain found in RING finger protein 14 (RNF14); RNF14, also called androgen receptor (AR) ...
 837-878 1.71e-07

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: 48.84  E-value: 1.71e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 296480493 837 CPR--CQSPAKYQPYKKRGLCSrtACGFDFCVLCLCAYHGSEEC 878
Cdd:cd20341   10 CPRpsCQTPVILEPDENLGICP--SCNYAFCTLCRETYHGVSPC 51
Rcat_RBR_parkin cd20357
Rcat domain found in parkin and similar proteins; Parkin, also called Parkinson juvenile ...
 830-878 1.55e-05

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: 43.15  E-value: 1.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296480493 830 IDEALKPCPRCQSPAkyqpyKKRG-----LCSRTACGFDFCVLCLCAYhgSEEC 878
Cdd:cd20357    3 IKKTTKPCPKCKVPT-----EKNGgcmhmKCPRPQCGLEWCWICGCEW--NRDC 49
IBR pfam01485
IBR domain, a half RING-finger domain; The IBR (In Between Ring fingers) domain is often found ...
 819-878 6.32e-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: 41.76  E-value: 6.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296480493  819 EEYVKVAKTLFIDEA--LKPCPR--CQSPAKYQPYKKRGL---CSRtaCGFDFCVLCLCAYHGSEEC 878
Cdd:pfam01485   1 EKYEKLLLKSYVESDpnLKWCPTpdCGYIIELTDGCSNTShvtCSK--CGHEFCFNCKEEWHEGLTC 65
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 113-209 7.63e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493 113 TSPPGTSARWARPPRGpqVGGSGDARCATPARPRPVGGVLGPARPPSASPAWGGSADRRAAWLKPPGRPLTSHPPTA--- 189
Cdd:PRK07764 369 DDERGLLARLERLERR--LGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSpag 446

                         90       100
                 ....*....|....*....|....
gi 296480493 190 ----PRAGDDRAAADPAWQSEKFP 209
Cdd:PRK07764 447 napaGGAPSPPPAAAPSAQPAPAP 470
PHA03247 PHA03247
large tegument protein UL36; Provisional
 69-202 1.27e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493   69 GGQFKPKEGKGGGPTRTRRGGCHSRASLGTRPRLLGGARAAAAHTSPPGTSARWARPPRGPQVGGsgdarCATPARPRPV 148
Cdd:PHA03247 2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGS-----LTSLADPPPP 2704

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 296480493  149 GGVLGPARPP--SASPAWGGSADRRAAWLKPPGRPLTSHPPTAPR--AGDDRAAADPA 202
Cdd:PHA03247 2705 PPTPEPAPHAlvSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpGGPARPARPPT 2762
Rcat_RBR_HHARI-like cd20356
Rcat domain found in human homolog of Drosophila Ariadne (HHARI) and similar proteins; This ...
 835-880 7.24e-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: 38.50  E-value: 7.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 296480493 835 KPCPRCQSPAKyqpykKRG-----LCSRTACGFDFCVLCLCAY--HGSE--ECSR 880
Cdd:cd20356    7 KECPKCHVTIE-----KNGgcnhmVCRNQNCKYEFCWVCLGPWepHGSSwyNCNR 56
FBOX smart00256
A Receptor for Ubiquitination Targets;
705-744 8.60e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 37.80  E-value: 8.60e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 296480493   705 HVLAMVLDSLTAESLCSVWKVSRNWREIIvqDKKANRRRK 744
Cdd:smart00256   4 EILEEILSKLDPKDLLRLRKVSRKWRSLI--DSHDFWFKL 41
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
88-204 1.06e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493  88 GGCHSRASLGTRPRLLGGARAAAAHTSPPGTSARWARPPRGPQVGGSGDARCATPARPRPV---------------GGVL 152
Cdd:PRK12323 369 GGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApealaaarqasargpGGAP 448

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296480493 153 GPARPPSASPAwgGSADRRAAWLKPPGRPLTSHPPTAPRAGDDRAAAD--PAWQ 204
Cdd:PRK12323 449 APAPAPAAAPA--AAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDdpPPWE 500
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 69-206 1.12e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493  69 GGQFKPK-----EGKGGGPTRTRRGGCHSRASLGTRPrllggaraaaahtSPPGTSARWARPPRGPQVGGSGDARCATPA 143
Cdd:PRK07764 579 GGDWQVEavvgpAPGAAGGEGPPAPASSGPPEEAARP-------------AAPAAPAAPAAPAPAGAAAAPAEASAAPAP 645

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493 144 RPRPVGGVL-GPARPPSASPAWGGSAD-----------------RRAAWLKPPGRPLTSHPPTAPRAGDDRAAADPAWQS 205
Cdd:PRK07764 646 GVAAPEHHPkHVAVPDASDGGDGWPAKaggaapaapppapapaaPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA 725


                 .
gi 296480493 206 E 206
Cdd:PRK07764 726 Q 726
PHA03378 PHA03378
EBNA-3B; Provisional
 115-202 1.31e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.75  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493 115 PPGTSARWARPPRG------PQVGGSGDAR--CATPARPRPVGGVLGPARPPSASpawggsadrraawlkpPGRPLTSHP 186
Cdd:PHA03378 716 RPAAATGRARPPAAapgrarPPAAAPGRARppAAAPGRARPPAAAPGRARPPAAA----------------PGAPTPQPP 779

                         90
                 ....*....|....*.
gi 296480493 187 PTAPRAGDDRAAADPA 202
Cdd:PHA03378 780 PQAPPAPQQRPRGAPT 795
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 25-202 1.48e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493  25 GVGAGKAETEPPGAGGAGGLRGRGAAAGGRKGRGGAARGGAVTQGGQFKP-KEGKGGGPTRTRRGGCHSRASLGTRPRLL 103
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAaPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493 104 GGARAAAahTSPPGTSARWARPPRGPQVGGSGDARCATPARPRPVGGvlgpARPPSASPAWGGSADRRAAWLKPPgRPLT 183
Cdd:PRK07764 672 KAGGAAP--AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADD----PAAQPPQAAQGASAPSPAADDPVP-LPPE 744

                        170
                 ....*....|....*....
gi 296480493 184 SHPPTAPRAGDDRAAADPA 202
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPA 763
IBR smart00647
In Between Ring fingers; the domains occurs between pairs og RING fingers
 834-878 1.49e-03

In Between Ring fingers; the domains occurs between pairs og RING fingers


Pssm-ID: 214763 [Multi-domain]  Cd Length: 64  Bit Score: 37.78  E-value: 1.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 296480493   834 LKPCPR--CQSPAKYQ--PYKKRGLCSrtACGFDFCVLCLCAYHGSEEC 878
Cdd:smart00647  18 LKWCPApdCSAAIIVTeeEGCNRVTCP--KCGFSFCFRCKVPWHSPVSC 64
F-box_FBXW1B cd22183
F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; ...
 693-733 1.60e-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: 37.19  E-value: 1.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 296480493 693 DILTELKYRNLKHVLAMVLDSLTAESLCSVWKVSRNWREII 733
Cdd:cd22183    3 DFITALPAKGLDHIAENILSYLDAESLCAAELVCKEWQRVI 43
Rcat_RBR_TRIAD1 cd20360
Rcat domain found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1); TRIAD1, ...
 835-885 1.70e-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: 37.37  E-value: 1.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296480493 835 KPCPRCQSpakyqPYKKRGLCSR---TACGFDFCVLCLCAY--HGSE--ECSRGAAKP 885
Cdd:cd20360    4 KDCPKCHV-----CIEKNGGCNHmqcSKCKHEFCWMCLGDWktHGSEyyECSRYKENP 56
Rcat_RBR_ARI7-like cd22583
Rcat domain found in E3 ubiquitin-protein ligase ARI7 and similar proteins; This subfamily ...
 835-875 1.92e-03

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: 37.04  E-value: 1.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 296480493 835 KPCPRCQSPAKyqpyKKRG---LCSRTACGFDFCVLCLCAY--HGS 875
Cdd:cd22583    3 KPCPKCKRPIE----KNQGcmhMTCSPPCKHEFCWLCLGPWseHGE 44
PHA03247 PHA03247
large tegument protein UL36; Provisional
 74-210 3.95e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480493   74 PKEGKGGGPTR--TRRGGCHSRASLGTRPRLLGGARAAAAHTSPPGTSARWARPprgpqVGGSGDARCATPARPRPVGGV 151
Cdd:PHA03247 2771 PPAAPAAGPPRrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP-----AGPLPPPTSAQPTAPPPPPGP 2845

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 296480493  152 LGPARPPSASPAWGGSADRRAAWLKPPGRPLTSHPPTAPRAgddrAAADPAWQSEKFPL 210
Cdd:PHA03247 2846 PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL----ARPAVSRSTESFAL 2900
Rcat_RBR_DEAH12-like cd22585
Rcat domain of ATP-dependent RNA helicase DEAH12 and similar proteins; This group includes ...
 835-878 8.93e-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: 8.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 296480493 835 KPCPRCQSPAkyqpyKKRGLCSR---TACGFDFCVLCLCAYHGSEEC 878
Cdd:cd22585    3 KRCPKCKSLI-----EKIDGCNHvtcTRCGTHICWVCLKVFETSSEC 44
 
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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