NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|509155805|ref|NP_001265341|]
View 

protein AMN1 homolog isoform 2 [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein; F-box protein( domain architecture ID 10174679)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions| F-box protein functions as the substrate-recognition component of a SCF (Skp1-Cullin-F-box protein) ubiquitin-protein ligase that is involved in ubiquitin-dependent degradation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 19-239 1.69e-97

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: 283.83  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  19 KDRLIKIMSMQGQITDSNISE---ILHPEVQTLDLRSCDISDAALLHLSNCRKLKKLNLNASKgnrvSVTSEGIKAVASS 95
Cdd:cd09293    1 KDPLLFILHKLGQITQSNISQllrILHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSK----LIDDEGLIALAQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  96 CSYLHEASLKRCCNLTDEGVVALALNCQLLKIIDLG---GCLSITDVSLHALGKNCPFLQCVDFSATQVSDSGVIALVSG 172
Cdd:cd09293   77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 509155805 173 pCAKKLEEIHMGHCVNLTDGAVEAVL--TYCPQIRILLFHGCPLITDHSREVLEQLVGP--NKLKQVTWTV 239
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 ...
 19-239 1.69e-97

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: 283.83  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  19 KDRLIKIMSMQGQITDSNISE---ILHPEVQTLDLRSCDISDAALLHLSNCRKLKKLNLNASKgnrvSVTSEGIKAVASS 95
Cdd:cd09293    1 KDPLLFILHKLGQITQSNISQllrILHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSK----LIDDEGLIALAQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  96 CSYLHEASLKRCCNLTDEGVVALALNCQLLKIIDLG---GCLSITDVSLHALGKNCPFLQCVDFSATQVSDSGVIALVSG 172
Cdd:cd09293   77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 509155805 173 pCAKKLEEIHMGHCVNLTDGAVEAVL--TYCPQIRILLFHGCPLITDHSREVLEQLVGP--NKLKQVTWTV 239
Cdd:cd09293  157 -CSKSLERLSLNNCRNLTDQSIPAILasNYFPNLSVLEFRGCPLITDFSRIILFKLWQPrlNKPILVEWCE 226
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 43-189 3.94e-05

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: 44.01  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  43 PEVQTLDLRSCDISDAALL----HLSNCRKLKKLNLNaskGNRVsvTSEGIKAVA---SSCSYLHEASLkRCCNLTDEGV 115
Cdd:COG5238  236 KSLTTLDLSNNQIGDEGVIalaeALKNNTTVETLYLS---GNQI--GAEGAIALAkalQGNTTLTSLDL-SVNRIGDEGA 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805 116 VALALNCQ---LLKIIDLGGClSITDVSLHALGKNC---PFLQCVDFSATQVSDSGVIALvsgpcAKKLEEIHMGHCVNL 189
Cdd:COG5238  310 IALAEGLQgnkTLHTLNLAYN-GIGAQGAIALAKALqenTTLHSLDLSDNQIGDEGAIAL-----AKYLEGNTTLRELNL 383
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 19-239 1.69e-97

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: 283.83  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  19 KDRLIKIMSMQGQITDSNISE---ILHPEVQTLDLRSCDISDAALLHLSNCRKLKKLNLNASKgnrvSVTSEGIKAVASS 95
Cdd:cd09293    1 KDPLLFILHKLGQITQSNISQllrILHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSK----LIDDEGLIALAQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  96 CSYLHEASLKRCCNLTDEGVVALALNCQLLKIIDLG---GCLSITDVSLHALGKNCPFLQCVDFSATQVSDSGVIALVSG 172
Cdd:cd09293   77 CPNLQVLDLRACENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 509155805 173 pCAKKLEEIHMGHCVNLTDGAVEAVL--TYCPQIRILLFHGCPLITDHSREVLEQLVGP--NKLKQVTWTV 239
Cdd:cd09293  157 -CSKSLERLSLNNCRNLTDQSIPAILasNYFPNLSVLEFRGCPLITDFSRIILFKLWQPrlNKPILVEWCE 226
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 43-189 3.94e-05

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: 44.01  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  43 PEVQTLDLRSCDISDAALL----HLSNCRKLKKLNLNaskGNRVsvTSEGIKAVA---SSCSYLHEASLkRCCNLTDEGV 115
Cdd:COG5238  236 KSLTTLDLSNNQIGDEGVIalaeALKNNTTVETLYLS---GNQI--GAEGAIALAkalQGNTTLTSLDL-SVNRIGDEGA 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805 116 VALALNCQ---LLKIIDLGGClSITDVSLHALGKNC---PFLQCVDFSATQVSDSGVIALvsgpcAKKLEEIHMGHCVNL 189
Cdd:COG5238  310 IALAEGLQgnkTLHTLNLAYN-GIGAQGAIALAKALqenTTLHSLDLSDNQIGDEGAIAL-----AKYLEGNTTLRELNL 383
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 62-218 3.48e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 37.46  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 509155805  62 HLSNCRKLKKLNLNaskGNRVSVTsEGikavasscsylheasLKRCCNLTDegvvaLALNCQLLkiiDLGGCLSITDVSL 141
Cdd:cd21340   63 NLENLVNLKKLYLG---GNRISVV-EG---------------LENLTNLEE-----LHIENQRL---PPGEKLTFDPRSL 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 509155805 142 HALGKNcpfLQCVDFSATQVSDSGVIAlvsgpCAKKLEEIHMGHCvNLTD-GAVEAVLTYCPQIRILLFHGCPLITDH 218
Cdd:cd21340  116 AALSNS---LRVLNISGNNIDSLEPLA-----PLRNLEQLDASNN-QISDlEELLDLLSSWPSLRELDLTGNPVCKKP 184
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH