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Conserved domains on  [gi|164663750|ref|NP_001106895|]
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protein AMN1 homolog isoform 1 [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 ...
 37-257 2.28e-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: 226.05  E-value: 2.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750  37 KDRLIKIMSIRGRITDSNISEV---LHPEVQRLDLRSCDISDVALQHLCKCRKLKALNLKSCREhrnsITSEGIKAVASS 113
Cdd:cd09293    1 KDPLLFILHKLGQITQSNISQLlriLHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKL----IDDEGLIALAQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750 114 CSDLHEIYLKGCCSVTDEGVLALALNCHLLKIIDLG---GCLGITDVSLHALGKNCPFLQCVDISTTQVSDNGVVALVSG 190
Cdd:cd09293   77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164663750 191 pCAKQLEEINMRYCINLTDKAVEA--ALTACPRICILLFHGCPLITDRSQEVLEQLIGSR--KLKQVTWSV 257
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 ...
 37-257 2.28e-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: 226.05  E-value: 2.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750  37 KDRLIKIMSIRGRITDSNISEV---LHPEVQRLDLRSCDISDVALQHLCKCRKLKALNLKSCREhrnsITSEGIKAVASS 113
Cdd:cd09293    1 KDPLLFILHKLGQITQSNISQLlriLHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKL----IDDEGLIALAQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750 114 CSDLHEIYLKGCCSVTDEGVLALALNCHLLKIIDLG---GCLGITDVSLHALGKNCPFLQCVDISTTQVSDNGVVALVSG 190
Cdd:cd09293   77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164663750 191 pCAKQLEEINMRYCINLTDKAVEA--ALTACPRICILLFHGCPLITDRSQEVLEQLIGSR--KLKQVTWSV 257
Cdd:cd09293  157 -CSKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLITDFSRIILFKLWQPRlnKPILVEWCE 226
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 63-249 5.65e-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: 40.93  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750  63 VQRLDLRSCDISDVALQHLCKCRKLKAlNLKSCREHRNSITSEGIKAVASSCSD---LHEIYLKGCCsVTDEGVLALA-- 137
Cdd:COG5238  182 VETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQ-IGDEGVIALAea 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750 138 -LNCHLLKIIDLGGClGITDVSLHALGK---NCPFLQCVDISTTQVSDNGVVALVSG-PCAKQLEEINMRYCiNLTDKAV 212
Cdd:COG5238  260 lKNNTTVETLYLSGN-QIGAEGAIALAKalqGNTTLTSLDLSVNRIGDEGAIALAEGlQGNKTLHTLNLAYN-GIGAQGA 337

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 164663750 213 EA---ALTACPRICILLFHGCPlITDRSQEVLEQLIGSRK 249
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 ...
 37-257 2.28e-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: 226.05  E-value: 2.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750  37 KDRLIKIMSIRGRITDSNISEV---LHPEVQRLDLRSCDISDVALQHLCKCRKLKALNLKSCREhrnsITSEGIKAVASS 113
Cdd:cd09293    1 KDPLLFILHKLGQITQSNISQLlriLHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKL----IDDEGLIALAQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750 114 CSDLHEIYLKGCCSVTDEGVLALALNCHLLKIIDLG---GCLGITDVSLHALGKNCPFLQCVDISTTQVSDNGVVALVSG 190
Cdd:cd09293   77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164663750 191 pCAKQLEEINMRYCINLTDKAVEA--ALTACPRICILLFHGCPLITDRSQEVLEQLIGSR--KLKQVTWSV 257
Cdd:cd09293  157 -CSKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLITDFSRIILFKLWQPRlnKPILVEWCE 226
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 64-227 1.07e-07

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: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750  64 QRLDLRSCDISDVALQHLCKCRKLKALNLKSCREHRNSITSEGIKAVA---SSCSDLHEIYLkGCCSVTDEGV----LAL 136
Cdd:cd00116  111 QELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAkalRANRDLKELNL-ANNGIGDAGIralaEGL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750 137 ALNCHlLKIIDLGGClGITDVSLHALG---KNCPFLQCVDISTTQVSDNGVVALVSG--PCAKQLEEINMrYCINLTDKA 211
Cdd:cd00116  190 KANCN-LEVLDLNNN-GLTDEGASALAetlASLKSLEVLNLGDNNLTDAGAAALASAllSPNISLLTLSL-SCNDITDDG 266

                        170
                 ....*....|....*.
gi 164663750 212 VEAALTACPRICILLF 227
Cdd:cd00116  267 AKDLAEVLAEKESLLE 282
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 63-249 5.65e-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: 40.93  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750  63 VQRLDLRSCDISDVALQHLCKCRKLKAlNLKSCREHRNSITSEGIKAVASSCSD---LHEIYLKGCCsVTDEGVLALA-- 137
Cdd:COG5238  182 VETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQ-IGDEGVIALAea 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663750 138 -LNCHLLKIIDLGGClGITDVSLHALGK---NCPFLQCVDISTTQVSDNGVVALVSG-PCAKQLEEINMRYCiNLTDKAV 212
Cdd:COG5238  260 lKNNTTVETLYLSGN-QIGAEGAIALAKalqGNTTLTSLDLSVNRIGDEGAIALAEGlQGNKTLHTLNLAYN-GIGAQGA 337

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 164663750 213 EA---ALTACPRICILLFHGCPlITDRSQEVLEQLIGSRK 249
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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