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Conserved domains on  [gi|1002288701|ref|XP_015648643|]
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putative F-box/LRR-repeat protein 23 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1001123)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; similar to Oryctolagus cuniculus monocyte differentiation antigen CD14, a coreceptor for bacterial lipopolysaccharide

Gene Ontology:  GO:0005515
PubMed:  11751054

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
60-157 2.13e-04

Leucine-rich repeat (LRR) protein [Transcription];


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002288701  60 KSCPQLKRFRLSQHGFHSFEDShdddealgIATMTQLRSLQIFGNTITNegLEAILDNCPHLESLDIRHCFNVFMDDTLr 139
Cdd:COG4886   156 GNLTNLKSLDLSNNQLTDLPEE--------LGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQLTDLPEPL- 224

                          90
                  ....*....|....*...
gi 1002288701 140 AKCARIKALRLPDDSIDD 157
Cdd:COG4886   225 ANLTNLETLDLSNNQLTD 242
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-157 2.13e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002288701  60 KSCPQLKRFRLSQHGFHSFEDShdddealgIATMTQLRSLQIFGNTITNegLEAILDNCPHLESLDIRHCFNVFMDDTLr 139
Cdd:COG4886   156 GNLTNLKSLDLSNNQLTDLPEE--------LGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQLTDLPEPL- 224

                          90
                  ....*....|....*...
gi 1002288701 140 AKCARIKALRLPDDSIDD 157
Cdd:COG4886   225 ANLTNLETLDLSNNQLTD 242
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 94-132 2.21e-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: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002288701  94 TQLRSLQIFGN-TITNEGLEAILDNCPHLESLDIRHCFNV 132
Cdd:cd09293    52 NKLKKLILPGSkLIDDEGLIALAQSCPNLQVLDLRACENI 91
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-157 2.13e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002288701  60 KSCPQLKRFRLSQHGFHSFEDShdddealgIATMTQLRSLQIFGNTITNegLEAILDNCPHLESLDIRHCFNVFMDDTLr 139
Cdd:COG4886   156 GNLTNLKSLDLSNNQLTDLPEE--------LGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQLTDLPEPL- 224

                          90
                  ....*....|....*...
gi 1002288701 140 AKCARIKALRLPDDSIDD 157
Cdd:COG4886   225 ANLTNLETLDLSNNQLTD 242
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 94-132 2.21e-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: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002288701  94 TQLRSLQIFGN-TITNEGLEAILDNCPHLESLDIRHCFNV 132
Cdd:cd09293    52 NKLKKLILPGSkLIDDEGLIALAQSCPNLQVLDLRACENI 91
 
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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