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Conserved domains on  [gi|1833563295|ref|NP_001368912|]
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protein AMN1 homolog isoform 3 [Mus musculus]

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 ...
 29-249 3.67e-74

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: 224.90  E-value: 3.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295  29 KDRLIKIMSIRGRITDSNISEV---LHPEVQRLDLRSCDISDVALQHLCKCRKLKALNLKSCREhrnsITSEGIKAVASS 105
Cdd:cd09293     1 KDPLLFILHKLGQITQSNISQLlriLHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKL----IDDEGLIALAQS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295 106 CSDLHEIYLKGCCSVTDEGVLALALNCHLLKIIDLG---GCLGITDVSLHALGKNCPFLQCVDISTTQVSDNGVVALVSG 182
Cdd:cd09293    77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833563295 183 pCAKQLEEINMRYCINLTDKAVEA--ALTACPRICILLFHGCPLITDRSQEVLEQLIGSR--KLKQVTWSV 249
Cdd:cd09293   157 -CSKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLITDFSRIILFKLWQPRlnKPILVEWCE 226
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 29-249 3.67e-74

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: 224.90  E-value: 3.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295  29 KDRLIKIMSIRGRITDSNISEV---LHPEVQRLDLRSCDISDVALQHLCKCRKLKALNLKSCREhrnsITSEGIKAVASS 105
Cdd:cd09293     1 KDPLLFILHKLGQITQSNISQLlriLHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKL----IDDEGLIALAQS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295 106 CSDLHEIYLKGCCSVTDEGVLALALNCHLLKIIDLG---GCLGITDVSLHALGKNCPFLQCVDISTTQVSDNGVVALVSG 182
Cdd:cd09293    77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833563295 183 pCAKQLEEINMRYCINLTDKAVEA--ALTACPRICILLFHGCPLITDRSQEVLEQLIGSR--KLKQVTWSV 249
Cdd:cd09293   157 -CSKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLITDFSRIILFKLWQPRlnKPILVEWCE 226
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 55-241 3.29e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 41.31  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295  55 VQRLDLRSCDISDVALQHLCKCRKLKAlNLKSCREHRNSITSEGIKAVASSCSD---LHEIYLKGCCsVTDEGVLALA-- 129
Cdd:COG5238   182 VETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQ-IGDEGVIALAea 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295 130 -LNCHLLKIIDLGGClGITDVSLHALGK---NCPFLQCVDISTTQVSDNGVVALVSG-PCAKQLEEINMRYCiNLTDKAV 204
Cdd:COG5238   260 lKNNTTVETLYLSGN-QIGAEGAIALAKalqGNTTLTSLDLSVNRIGDEGAIALAEGlQGNKTLHTLNLAYN-GIGAQGA 337

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1833563295 205 EA---ALTACPRICILLFHGCPlITDRSQEVLEQLIGSRK 241
Cdd:COG5238   338 IAlakALQENTTLHSLDLSDNQ-IGDEGAIALAKYLEGNT 376
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 29-249 3.67e-74

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: 224.90  E-value: 3.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295  29 KDRLIKIMSIRGRITDSNISEV---LHPEVQRLDLRSCDISDVALQHLCKCRKLKALNLKSCREhrnsITSEGIKAVASS 105
Cdd:cd09293     1 KDPLLFILHKLGQITQSNISQLlriLHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKL----IDDEGLIALAQS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295 106 CSDLHEIYLKGCCSVTDEGVLALALNCHLLKIIDLG---GCLGITDVSLHALGKNCPFLQCVDISTTQVSDNGVVALVSG 182
Cdd:cd09293    77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833563295 183 pCAKQLEEINMRYCINLTDKAVEA--ALTACPRICILLFHGCPLITDRSQEVLEQLIGSR--KLKQVTWSV 249
Cdd:cd09293   157 -CSKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLITDFSRIILFKLWQPRlnKPILVEWCE 226
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 56-219 7.80e-08

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 51.97  E-value: 7.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295  56 QRLDLRSCDISDVALQHLCKCRKLKALNLKSCREHRNSITSEGIKAVA---SSCSDLHEIYLkGCCSVTDEGV----LAL 128
Cdd:cd00116   111 QELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAkalRANRDLKELNL-ANNGIGDAGIralaEGL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295 129 ALNCHlLKIIDLGGClGITDVSLHALG---KNCPFLQCVDISTTQVSDNGVVALVSG--PCAKQLEEINMrYCINLTDKA 203
Cdd:cd00116   190 KANCN-LEVLDLNNN-GLTDEGASALAetlASLKSLEVLNLGDNNLTDAGAAALASAllSPNISLLTLSL-SCNDITDDG 266

                         170
                  ....*....|....*.
gi 1833563295 204 VEAALTACPRICILLF 219
Cdd:cd00116   267 AKDLAEVLAEKESLLE 282
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 55-241 3.29e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 41.31  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295  55 VQRLDLRSCDISDVALQHLCKCRKLKAlNLKSCREHRNSITSEGIKAVASSCSD---LHEIYLKGCCsVTDEGVLALA-- 129
Cdd:COG5238   182 VETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQ-IGDEGVIALAea 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563295 130 -LNCHLLKIIDLGGClGITDVSLHALGK---NCPFLQCVDISTTQVSDNGVVALVSG-PCAKQLEEINMRYCiNLTDKAV 204
Cdd:COG5238   260 lKNNTTVETLYLSGN-QIGAEGAIALAKalqGNTTLTSLDLSVNRIGDEGAIALAEGlQGNKTLHTLNLAYN-GIGAQGA 337

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1833563295 205 EA---ALTACPRICILLFHGCPlITDRSQEVLEQLIGSRK 241
Cdd:COG5238   338 IAlakALQENTTLHSLDLSDNQ-IGDEGAIALAKYLEGNT 376
 
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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