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Conserved domains on  [gi|15236356|ref|NP_192272|]
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RNI-like superfamily protein [Arabidopsis thaliana]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1563018)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

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 ...
 39-179 1.01e-05

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: 45.01  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236356  39 GCVEIniehfgTDSLLTYIADRSSNLRHLGLAKCDQITGMGLFTEAMKLPLLEDLELSYC----LIKGKNLEAIGFACLH 114
Cdd:cd09293  61 GSKLI------DDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHrnghLITDVSLSALGKNCTF 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236356 115 LKTLklncqGFKFPGFTydhD------ALGIAKRMPEL---RCLQLfgnrvSDVGLNAIF--DGCPHLEHLDLRQC 179
Cdd:cd09293 135 LQTV-----GFAGCDVT---DkgvwelASGCSKSLERLslnNCRNL-----TDQSIPAILasNYFPNLSVLEFRGC 197
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 39-179 1.01e-05

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: 45.01  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236356  39 GCVEIniehfgTDSLLTYIADRSSNLRHLGLAKCDQITGMGLFTEAMKLPLLEDLELSYC----LIKGKNLEAIGFACLH 114
Cdd:cd09293  61 GSKLI------DDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHrnghLITDVSLSALGKNCTF 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236356 115 LKTLklncqGFKFPGFTydhD------ALGIAKRMPEL---RCLQLfgnrvSDVGLNAIF--DGCPHLEHLDLRQC 179
Cdd:cd09293 135 LQTV-----GFAGCDVT---DkgvwelASGCSKSLERLslnNCRNL-----TDQSIPAILasNYFPNLSVLEFRGC 197
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 144-190 3.14e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 34.53  E-value: 3.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15236356   144 PELRCLQLFGNRVSDVGLnaiFDGCPHLEHLDLRQCFNINLVGDLEK 190
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP---LAKLPNLETLDLSGNNKITDLSDLAN 44
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 39-179 1.01e-05

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: 45.01  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236356  39 GCVEIniehfgTDSLLTYIADRSSNLRHLGLAKCDQITGMGLFTEAMKLPLLEDLELSYC----LIKGKNLEAIGFACLH 114
Cdd:cd09293  61 GSKLI------DDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHrnghLITDVSLSALGKNCTF 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236356 115 LKTLklncqGFKFPGFTydhD------ALGIAKRMPEL---RCLQLfgnrvSDVGLNAIF--DGCPHLEHLDLRQC 179
Cdd:cd09293 135 LQTV-----GFAGCDVT---DkgvwelASGCSKSLERLslnNCRNL-----TDQSIPAILasNYFPNLSVLEFRGC 197
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 43-182 1.22e-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: 41.54  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236356  43 INIEHFGTDSLLTYIADRSS----------NLRHLGLAKCDQITGMGLFTEAMKLPLLEDLELSYC-LIKGKNLEAIGFA 111
Cdd:cd09293  23 LRILHSGLEWLELYMCPISDppldqlsncnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACeNITDSGIVALATN 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236356 112 CLHLKTLKL----NCQGFKfpgftyDHDALGIAKRMPELRCLQLFGNRVSDVGLNAIFDGC-PHLEHLDLRQCFNI 182
Cdd:cd09293 103 CPKLQTINLgrhrNGHLIT------DVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGCsKSLERLSLNNCRNL 172
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 144-190 3.14e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 34.53  E-value: 3.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15236356   144 PELRCLQLFGNRVSDVGLnaiFDGCPHLEHLDLRQCFNINLVGDLEK 190
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP---LAKLPNLETLDLSGNNKITDLSDLAN 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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