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Conserved domains on  [gi|30682042|ref|NP_196384|]
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RNI-like superfamily protein [Arabidopsis thaliana]

Protein Classification

F-box/LRR-repeat protein( domain architecture ID 1903223)

F-box/LRR-repeat protein functions as the substrate-recognition component of a SCF (Skp1-Cullin-F-box protein) ubiquitin-protein ligase that is involved in ubiquitin-dependent degradation

CATH:  1.20.1280.50
Gene Ontology:  GO:0019005|GO:0005515|GO:0006511|GO:0016567
PubMed:  31898225|11178263|14747988|7583641|11751054|10581972
SCOP:  4001927

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 206-361 1.07e-09

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 58.49  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 206 ECSRLQELELHKC--SDSVLLGIGAFENLQILRLVGNVdglynsLVSDIGLMILAQGCKRLVKLELVGCEGGFD-GIKEI 282
Cdd:cd09293  26 LHSGLEWLELYMCpiSDPPLDQLSNCNKLKKLILPGSK------LIDDEGLIALAQSCPNLQVLDLRACENITDsGIVAL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 283 GECCQMLEELTVCDNKMESGWLGG-----LRYCENLKTLKLVSCKKIDNDPDESLSCCCPALERLQLEKCQLRDKNTVKA 357
Cdd:cd09293 100 ATNCPKLQTINLGRHRNGHLITDVslsalGKNCTFLQTVGFAGCDVTDKGVWELASGCSKSLERLSLNNCRNLTDQSIPA 179


                ....
gi 30682042 358 LFKM 361
Cdd:cd09293 180 ILAS 183
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 64-95 1.04e-04

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 cd22159:

Pssm-ID: 459239  Cd Length: 40  Bit Score: 39.37  E-value: 1.04e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 30682042  64 LLPDLILIRVIQKIPNSQ-RKNLSLVCKRWFRL 95
Cdd:cd22159   3 LLPDEILELIFSYLSDPWdRNSCSLVCKRWYRL 35
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 291-433 5.85e-04

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 41.16  E-value: 5.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 291 ELTVCDNKMESgwLGGLRYCENLKTLKLVSCKKIDNDPDESLSCCCPALERLQLEKCQLRDKNTVKALFKMCEAAREIVF 370
Cdd:cd09293  34 ELYMCPISDPP--LDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINL 111

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682042 371 ---QDCWGL-DNDIFSLAMAFGRVKLLYLEGCSLLTTSGLESVILHWHELEHLKVVSCKNIKDSEVS 433
Cdd:cd09293 112 grhRNGHLItDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGCSKSLERLSLNNCRNLTDQSIP 178
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 206-361 1.07e-09

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 58.49  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 206 ECSRLQELELHKC--SDSVLLGIGAFENLQILRLVGNVdglynsLVSDIGLMILAQGCKRLVKLELVGCEGGFD-GIKEI 282
Cdd:cd09293  26 LHSGLEWLELYMCpiSDPPLDQLSNCNKLKKLILPGSK------LIDDEGLIALAQSCPNLQVLDLRACENITDsGIVAL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 283 GECCQMLEELTVCDNKMESGWLGG-----LRYCENLKTLKLVSCKKIDNDPDESLSCCCPALERLQLEKCQLRDKNTVKA 357
Cdd:cd09293 100 ATNCPKLQTINLGRHRNGHLITDVslsalGKNCTFLQTVGFAGCDVTDKGVWELASGCSKSLERLSLNNCRNLTDQSIPA 179


                ....
gi 30682042 358 LFKM 361
Cdd:cd09293 180 ILAS 183
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 64-95 1.04e-04

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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: 438930  Cd Length: 40  Bit Score: 39.37  E-value: 1.04e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 30682042  64 LLPDLILIRVIQKIPNSQ-RKNLSLVCKRWFRL 95
Cdd:cd22159   3 LLPDEILELIFSYLSDPWdRNSCSLVCKRWYRL 35
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 291-433 5.85e-04

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 41.16  E-value: 5.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 291 ELTVCDNKMESgwLGGLRYCENLKTLKLVSCKKIDNDPDESLSCCCPALERLQLEKCQLRDKNTVKALFKMCEAAREIVF 370
Cdd:cd09293  34 ELYMCPISDPP--LDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINL 111

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682042 371 ---QDCWGL-DNDIFSLAMAFGRVKLLYLEGCSLLTTSGLESVILHWHELEHLKVVSCKNIKDSEVS 433
Cdd:cd09293 112 grhRNGHLItDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGCSKSLERLSLNNCRNLTDQSIP 178
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 206-361 1.07e-09

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 58.49  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 206 ECSRLQELELHKC--SDSVLLGIGAFENLQILRLVGNVdglynsLVSDIGLMILAQGCKRLVKLELVGCEGGFD-GIKEI 282
Cdd:cd09293  26 LHSGLEWLELYMCpiSDPPLDQLSNCNKLKKLILPGSK------LIDDEGLIALAQSCPNLQVLDLRACENITDsGIVAL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 283 GECCQMLEELTVCDNKMESGWLGG-----LRYCENLKTLKLVSCKKIDNDPDESLSCCCPALERLQLEKCQLRDKNTVKA 357
Cdd:cd09293 100 ATNCPKLQTINLGRHRNGHLITDVslsalGKNCTFLQTVGFAGCDVTDKGVWELASGCSKSLERLSLNNCRNLTDQSIPA 179


                ....
gi 30682042 358 LFKM 361
Cdd:cd09293 180 ILAS 183
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 184-324 9.07e-07

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 49.63  E-value: 9.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 184 CSNLRKLVVTN----TSElGLLNVAEECSRLQELELHKC---SDSVLLGIGAF-ENLQILRLVGNVDGlynSLVSDIGLM 255
Cdd:cd09293  51 CNKLKKLILPGskliDDE-GLIALAQSCPNLQVLDLRACeniTDSGIVALATNcPKLQTINLGRHRNG---HLITDVSLS 126

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682042 256 ILAQGCKRLVKLELVGCEGGFDGIKEIG-ECCQMLEELTV--CDNKMESG--WLGGLRYCENLKTLKLVSCKKI 324
Cdd:cd09293 127 ALGKNCTFLQTVGFAGCDVTDKGVWELAsGCSKSLERLSLnnCRNLTDQSipAILASNYFPNLSVLEFRGCPLI 200
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 64-95 1.04e-04

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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: 438930  Cd Length: 40  Bit Score: 39.37  E-value: 1.04e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 30682042  64 LLPDLILIRVIQKIPNSQ-RKNLSLVCKRWFRL 95
Cdd:cd22159   3 LLPDEILELIFSYLSDPWdRNSCSLVCKRWYRL 35
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 291-433 5.85e-04

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 41.16  E-value: 5.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682042 291 ELTVCDNKMESgwLGGLRYCENLKTLKLVSCKKIDNDPDESLSCCCPALERLQLEKCQLRDKNTVKALFKMCEAAREIVF 370
Cdd:cd09293  34 ELYMCPISDPP--LDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINL 111

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682042 371 ---QDCWGL-DNDIFSLAMAFGRVKLLYLEGCSLLTTSGLESVILHWHELEHLKVVSCKNIKDSEVS 433
Cdd:cd09293 112 grhRNGHLItDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGCSKSLERLSLNNCRNLTDQSIP 178
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 65-106 9.13e-03

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, 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. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. 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: 438876  Cd Length: 48  Bit Score: 34.15  E-value: 9.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 30682042  65 LPDLILIRVIQKIPNSQRKNLSLVCKRWFR--LHGRLVRSFKVS 106
Cdd:cd22104   4 LPSVVLVHIFSYLPPRDRLRASSTCRRWREalFHPSLWRSLRLH 47
 
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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