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Conserved domains on  [gi|1785378033|ref|XP_012821959|]
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F-box/LRR-repeat protein 15 isoform X1 [Xenopus tropicalis]

Protein Classification

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 ...
 65-251 1.84e-13

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: 68.12  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785378033  65 SHLPKSTFSELLRNN-TVLQKLDLQSCcdwltDKELLPVIGQNH--HLIHINLNSCGQLTRQSLVAISLSCPHLQNICLG 141
Cdd:cd09293    12 GQITQSNISQLLRILhSGLEWLELYMC-----PISDPPLDQLSNcnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785378033 142 HCEWVDCLSLRSLVDHCKCLEAIDL---TACRQLKDDTISYLVQKSTRLKSLSLAvNANISDIAVEETAKNCRD-LEHLD 217
Cdd:cd09293    87 ACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFA-GCDVTDKGVWELASGCSKsLERLS 165

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1785378033 218 LTGCLRVKNDSIRTLAE--YCTKLKSLKVKHCHNVT 251
Cdd:cd09293   166 LNNCRNLTDQSIPAILAsnYFPNLSVLEFRGCPLIT 201
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 12-55 6.46e-13

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 61.75  E-value: 6.46e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1785378033  12 LLDLPWEDVLVPHILRNLPLRHILSLQRVSKPFQSLVHLYLANC 55
Cdd:cd22126     1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFSKL 44
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 65-251 1.84e-13

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: 68.12  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785378033  65 SHLPKSTFSELLRNN-TVLQKLDLQSCcdwltDKELLPVIGQNH--HLIHINLNSCGQLTRQSLVAISLSCPHLQNICLG 141
Cdd:cd09293    12 GQITQSNISQLLRILhSGLEWLELYMC-----PISDPPLDQLSNcnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785378033 142 HCEWVDCLSLRSLVDHCKCLEAIDL---TACRQLKDDTISYLVQKSTRLKSLSLAvNANISDIAVEETAKNCRD-LEHLD 217
Cdd:cd09293    87 ACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFA-GCDVTDKGVWELASGCSKsLERLS 165

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1785378033 218 LTGCLRVKNDSIRTLAE--YCTKLKSLKVKHCHNVT 251
Cdd:cd09293   166 LNNCRNLTDQSIPAILAsnYFPNLSVLEFRGCPLIT 201
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 12-55 6.46e-13

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 61.75  E-value: 6.46e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1785378033  12 LLDLPWEDVLVPHILRNLPLRHILSLQRVSKPFQSLVHLYLANC 55
Cdd:cd22126     1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFSKL 44
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 65-251 1.84e-13

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: 68.12  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785378033  65 SHLPKSTFSELLRNN-TVLQKLDLQSCcdwltDKELLPVIGQNH--HLIHINLNSCGQLTRQSLVAISLSCPHLQNICLG 141
Cdd:cd09293    12 GQITQSNISQLLRILhSGLEWLELYMC-----PISDPPLDQLSNcnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785378033 142 HCEWVDCLSLRSLVDHCKCLEAIDL---TACRQLKDDTISYLVQKSTRLKSLSLAvNANISDIAVEETAKNCRD-LEHLD 217
Cdd:cd09293    87 ACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFA-GCDVTDKGVWELASGCSKsLERLS 165

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1785378033 218 LTGCLRVKNDSIRTLAE--YCTKLKSLKVKHCHNVT 251
Cdd:cd09293   166 LNNCRNLTDQSIPAILAsnYFPNLSVLEFRGCPLIT 201
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 12-55 6.46e-13

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 61.75  E-value: 6.46e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1785378033  12 LLDLPWEDVLVPHILRNLPLRHILSLQRVSKPFQSLVHLYLANC 55
Cdd:cd22126     1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFSKL 44
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 184-255 1.75e-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: 50.79  E-value: 1.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785378033 184 STRLKSLSLAVNANISDIAVEETAKNCRDLEHLDLTGCLRVKNDSIRTLAEYCTKLKSLKV---KHCHNVTESSL 255
Cdd:cd09293    51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSL 125
 
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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