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Conserved domains on  [gi|1571052967|ref|NP_001355338|]
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leucine-rich repeat-containing protein 29 isoform 2 [Mus musculus]

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 ...
 240-444 3.65e-10

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: 60.03  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 240 PEALQALGQVT-GLKLEELYLHSCRDLSSEAVTILCRQQPGLTSLDLSGCSDLTDGALLAVSRGLRHLRHLSLKKLQR-- 316
Cdd:cd09293    39 PISDPPLDQLSnCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNgh 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 317 -LTDAGCAALGAL-RELQSLDMAECclvsgrelaQVlgsvrrapraltslrlaycsslkvlqfpqlrqlslsllpafTDT 394
Cdd:cd09293   119 lITDVSLSALGKNcTFLQTVGFAGC---------DV-----------------------------------------TDK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1571052967 395 GLVAVARGC-PSLERLTLSHCSHLSDEGWAQ--AARLWPRLQHLNLSSCSQLT 444
Cdd:cd09293   149 GVWELASGCsKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLIT 201
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 403-487 8.87e-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.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 50.02  E-value: 8.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 403 CPSLERLTLSHCSHLSDEGWAQAARLWPRLQHLNLSSCSQLTEQTLDTIGQACKQLRVLDV---AMCPGINMAAVRHFQA 479
Cdd:cd09293    51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130


                  ....*...
gi 1571052967 480 QLPQVTCI 487
Cdd:cd09293   131 NCTFLQTV 138
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 118-360 5.69e-05

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.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 45.04  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 118 CPVLRTLDLSGCNSLFTSGTLLAQpetaqCVREALSGLRDLNLAGLRDL-TDLSFNHLSSCFPSLERLSLAYCHLSFELS 196
Cdd:cd00116    80 GCGLQELDLSDNALGPDGCGVLES-----LLRSSSLQELKLNNNGLGDRgLRLLAKGLKDLPPALEKLVLGRNRLEGASC 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 197 PTWGsispqvsspsqlsfhNLLKFIkeraGTLRALDLSGTGLPPEALQALGQvtGLK----LEELYLHSC--RDLSSEAV 270
Cdd:cd00116   155 EALA---------------KALRAN----RDLKELNLANNGIGDAGIRALAE--GLKancnLEVLDLNNNglTDEGASAL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 271 TILCRQQPGLTSLDLSGCSdLTDGALLAVSRGLRHLRHlSLKKLQ----RLTDAGCAAL-GALRE---LQSLDMAECCLv 342
Cdd:cd00116   214 AETLASLKSLEVLNLGDNN-LTDAGAAALASALLSPNI-SLLTLSlscnDITDDGAKDLaEVLAEkesLLELDLRGNKF- 290

                         250
                  ....*....|....*...
gi 1571052967 343 sGRELAQVLGSVRRAPRA 360
Cdd:cd00116   291 -GEEGAQLLAESLLEPGN 307
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 2-33 5.85e-04

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. 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. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


The actual alignment was detected with superfamily member cd22104:

Pssm-ID: 459239  Cd Length: 48  Bit Score: 37.62  E-value: 5.85e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1571052967   2 ADSLPLEMLTYILSFLPLSDQKEASLVSRTWY 33
Cdd:cd22104     1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWR 32
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 240-444 3.65e-10

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: 60.03  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 240 PEALQALGQVT-GLKLEELYLHSCRDLSSEAVTILCRQQPGLTSLDLSGCSDLTDGALLAVSRGLRHLRHLSLKKLQR-- 316
Cdd:cd09293    39 PISDPPLDQLSnCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNgh 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 317 -LTDAGCAALGAL-RELQSLDMAECclvsgrelaQVlgsvrrapraltslrlaycsslkvlqfpqlrqlslsllpafTDT 394
Cdd:cd09293   119 lITDVSLSALGKNcTFLQTVGFAGC---------DV-----------------------------------------TDK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1571052967 395 GLVAVARGC-PSLERLTLSHCSHLSDEGWAQ--AARLWPRLQHLNLSSCSQLT 444
Cdd:cd09293   149 GVWELASGCsKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLIT 201
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 403-487 8.87e-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: 50.02  E-value: 8.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 403 CPSLERLTLSHCSHLSDEGWAQAARLWPRLQHLNLSSCSQLTEQTLDTIGQACKQLRVLDV---AMCPGINMAAVRHFQA 479
Cdd:cd09293    51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130


                  ....*...
gi 1571052967 480 QLPQVTCI 487
Cdd:cd09293   131 NCTFLQTV 138
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 224-464 6.55e-06

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 48.58  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 224 RAGTLRALDLSGTGLPPEAL-QALG------------QVTGLKLEELYLHSCRDLSSeavtilcrqqpgLTSLDLSGC-- 288
Cdd:pfam19729 205 KNVSLEALQLPRSWLNGSSLlQHLKfsnpfylsfsrcTLSGGQLIQRVLNGGKDLRS------------LVSLNLSGCvh 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 289 ------------SDLTDGALLAVSRGLRHLRHLSLKKLQRLTDAG-----CAALGALRELQSLDMAECCLVSGRELAQVl 351
Cdd:pfam19729 273 cllpdsllrkaeDDIDSSIVETLVACCPNLRHLNLSAAHHHSSEGlgghlCALLARLKHLRSLSLPVCAVADSAKTADK- 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 352 gSVRRAPRALTSLRLAYCSSLKVlQFPQLRQLSLSLLPAFTDTGLVAVARGCPSLERLTL-------------------- 411
Cdd:pfam19729 352 -SPSQTDLASSAVPLGFGKKVRI-GVQTYPRDSSEQASPDPTSVFWTLLKGCPFLEELELigsnfssamprnepairnsl 429

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1571052967 412 ---SHCSHLSDEGWAQAARLwPRLQHLNLSSC-SQLTEQTLDTIGQACKQLRVLDVA 464
Cdd:pfam19729 430 ppcARAQSVGDSEVAAIGQL-AFLRRLTLAQLpGILTGSGLVQIGLQCQDLQVLSLA 485
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 118-360 5.69e-05

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: 45.04  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 118 CPVLRTLDLSGCNSLFTSGTLLAQpetaqCVREALSGLRDLNLAGLRDL-TDLSFNHLSSCFPSLERLSLAYCHLSFELS 196
Cdd:cd00116    80 GCGLQELDLSDNALGPDGCGVLES-----LLRSSSLQELKLNNNGLGDRgLRLLAKGLKDLPPALEKLVLGRNRLEGASC 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 197 PTWGsispqvsspsqlsfhNLLKFIkeraGTLRALDLSGTGLPPEALQALGQvtGLK----LEELYLHSC--RDLSSEAV 270
Cdd:cd00116   155 EALA---------------KALRAN----RDLKELNLANNGIGDAGIRALAE--GLKancnLEVLDLNNNglTDEGASAL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 271 TILCRQQPGLTSLDLSGCSdLTDGALLAVSRGLRHLRHlSLKKLQ----RLTDAGCAAL-GALRE---LQSLDMAECCLv 342
Cdd:cd00116   214 AETLASLKSLEVLNLGDNN-LTDAGAAALASALLSPNI-SLLTLSlscnDITDDGAKDLaEVLAEkesLLELDLRGNKF- 290

                         250
                  ....*....|....*...
gi 1571052967 343 sGRELAQVLGSVRRAPRA 360
Cdd:cd00116   291 -GEEGAQLLAESLLEPGN 307
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 2-33 5.85e-04

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, 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 target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. 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: 438876  Cd Length: 48  Bit Score: 37.62  E-value: 5.85e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1571052967   2 ADSLPLEMLTYILSFLPLSDQKEASLVSRTWY 33
Cdd:cd22104     1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWR 32
FBOX smart00256
A Receptor for Ubiquitination Targets;
5-38 1.09e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.65  E-value: 1.09e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1571052967    5 LPLEMLTYILSFLPLSDQKEASLVSRTWYCAAQN 38
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDS 34
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 3-38 1.17e-03

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 36.69  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1571052967   3 DSLPLEMLTYILSFLPLSDQKEASLVSRTWYCAAQN 38
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASD 37
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 227-338 5.58e-03

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: 39.00  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 227 TLRALDLSGTGLPPEALQALGQV--TGLKLEELYLhSCRDLSSEAVTILC---RQQPGLTSLDLSGcSDLTDGALLAVSR 301
Cdd:COG5238   237 SLTTLDLSNNQIGDEGVIALAEAlkNNTTVETLYL-SGNQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDEGAIALAE 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1571052967 302 GLRH---LRHLSLKKlQRLTDAGC----AALGALRELQSLDMAE 338
Cdd:COG5238   315 GLQGnktLHTLNLAY-NGIGAQGAialaKALQENTTLHSLDLSD 357
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 240-444 3.65e-10

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: 60.03  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 240 PEALQALGQVT-GLKLEELYLHSCRDLSSEAVTILCRQQPGLTSLDLSGCSDLTDGALLAVSRGLRHLRHLSLKKLQR-- 316
Cdd:cd09293    39 PISDPPLDQLSnCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNgh 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 317 -LTDAGCAALGAL-RELQSLDMAECclvsgrelaQVlgsvrrapraltslrlaycsslkvlqfpqlrqlslsllpafTDT 394
Cdd:cd09293   119 lITDVSLSALGKNcTFLQTVGFAGC---------DV-----------------------------------------TDK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1571052967 395 GLVAVARGC-PSLERLTLSHCSHLSDEGWAQ--AARLWPRLQHLNLSSCSQLT 444
Cdd:cd09293   149 GVWELASGCsKSLERLSLNNCRNLTDQSIPAilASNYFPNLSVLEFRGCPLIT 201
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 254-469 7.37e-10

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: 59.26  E-value: 7.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 254 LEELYLHSCRDLSSEAVTILCRQQpgLTSLDLSGCSDLTDGALLAVSRGLRHLRHLSLKKLQRLTDAGCAALGA-LRELQ 332
Cdd:cd09293    30 LEWLELYMCPISDPPLDQLSNCNK--LKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 333 SLDmaecclvsgrelaqvLGSVRRapraltslrlayCSSLkvlqfpqlrqlslsllpafTDTGLVAVARGCPSLERLTLS 412
Cdd:cd09293   108 TIN---------------LGRHRN------------GHLI-------------------TDVSLSALGKNCTFLQTVGFA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 413 HCsHLSDEG-WAQAARLWPRLQHLNLSSCSQLTEQTLDTI--GQACKQLRVLDVAMCPGI 469
Cdd:cd09293   142 GC-DVTDKGvWELASGCSKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLI 200
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 403-487 8.87e-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: 50.02  E-value: 8.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 403 CPSLERLTLSHCSHLSDEGWAQAARLWPRLQHLNLSSCSQLTEQTLDTIGQACKQLRVLDV---AMCPGINMAAVRHFQA 479
Cdd:cd09293    51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130


                  ....*...
gi 1571052967 480 QLPQVTCI 487
Cdd:cd09293   131 NCTFLQTV 138
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 224-464 6.55e-06

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 48.58  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 224 RAGTLRALDLSGTGLPPEAL-QALG------------QVTGLKLEELYLHSCRDLSSeavtilcrqqpgLTSLDLSGC-- 288
Cdd:pfam19729 205 KNVSLEALQLPRSWLNGSSLlQHLKfsnpfylsfsrcTLSGGQLIQRVLNGGKDLRS------------LVSLNLSGCvh 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 289 ------------SDLTDGALLAVSRGLRHLRHLSLKKLQRLTDAG-----CAALGALRELQSLDMAECCLVSGRELAQVl 351
Cdd:pfam19729 273 cllpdsllrkaeDDIDSSIVETLVACCPNLRHLNLSAAHHHSSEGlgghlCALLARLKHLRSLSLPVCAVADSAKTADK- 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 352 gSVRRAPRALTSLRLAYCSSLKVlQFPQLRQLSLSLLPAFTDTGLVAVARGCPSLERLTL-------------------- 411
Cdd:pfam19729 352 -SPSQTDLASSAVPLGFGKKVRI-GVQTYPRDSSEQASPDPTSVFWTLLKGCPFLEELELigsnfssamprnepairnsl 429

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1571052967 412 ---SHCSHLSDEGWAQAARLwPRLQHLNLSSC-SQLTEQTLDTIGQACKQLRVLDVA 464
Cdd:pfam19729 430 ppcARAQSVGDSEVAAIGQL-AFLRRLTLAQLpGILTGSGLVQIGLQCQDLQVLSLA 485
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 118-360 5.69e-05

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: 45.04  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 118 CPVLRTLDLSGCNSLFTSGTLLAQpetaqCVREALSGLRDLNLAGLRDL-TDLSFNHLSSCFPSLERLSLAYCHLSFELS 196
Cdd:cd00116    80 GCGLQELDLSDNALGPDGCGVLES-----LLRSSSLQELKLNNNGLGDRgLRLLAKGLKDLPPALEKLVLGRNRLEGASC 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 197 PTWGsispqvsspsqlsfhNLLKFIkeraGTLRALDLSGTGLPPEALQALGQvtGLK----LEELYLHSC--RDLSSEAV 270
Cdd:cd00116   155 EALA---------------KALRAN----RDLKELNLANNGIGDAGIRALAE--GLKancnLEVLDLNNNglTDEGASAL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 271 TILCRQQPGLTSLDLSGCSdLTDGALLAVSRGLRHLRHlSLKKLQ----RLTDAGCAAL-GALRE---LQSLDMAECCLv 342
Cdd:cd00116   214 AETLASLKSLEVLNLGDNN-LTDAGAAALASALLSPNI-SLLTLSlscnDITDDGAKDLaEVLAEkesLLELDLRGNKF- 290

                         250
                  ....*....|....*...
gi 1571052967 343 sGRELAQVLGSVRRAPRA 360
Cdd:cd00116   291 -GEEGAQLLAESLLEPGN 307
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 2-33 5.85e-04

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, 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 target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. 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: 438876  Cd Length: 48  Bit Score: 37.62  E-value: 5.85e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1571052967   2 ADSLPLEMLTYILSFLPLSDQKEASLVSRTWY 33
Cdd:cd22104     1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWR 32
FBOX smart00256
A Receptor for Ubiquitination Targets;
5-38 1.09e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.65  E-value: 1.09e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1571052967    5 LPLEMLTYILSFLPLSDQKEASLVSRTWYCAAQN 38
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDS 34
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 3-38 1.17e-03

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 36.69  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1571052967   3 DSLPLEMLTYILSFLPLSDQKEASLVSRTWYCAAQN 38
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASD 37
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 85-191 1.60e-03

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: 40.00  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967  85 LQSVAYHLgPHLESLCLG----GGSPTEASFLALILGCPVLRTLDLSGCNSlftsgtllaqpeTAQCVREALSG----LR 156
Cdd:cd09293    96 IVALATNC-PKLQTINLGrhrnGHLITDVSLSALGKNCTFLQTVGFAGCDV------------TDKGVWELASGcsksLE 162

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1571052967 157 DLNLAGLRDLTDLSFNHL--SSCFPSLERLSLAYCHL 191
Cdd:cd09293   163 RLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPL 199
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 3-37 1.84e-03

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. 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. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 35.88  E-value: 1.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1571052967   3 DSLPLEMLTYILSFLPLSDQKEASLVSRTWYCAAQ 37
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 3-38 2.29e-03

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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: 425796  Cd Length: 43  Bit Score: 35.98  E-value: 2.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1571052967   3 DSLPLEMLTYILSFLPLSDQKEASLVSRTWYCAAQN 38
Cdd:pfam00646   2 LDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDS 37
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 4-36 2.78e-03

F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also called F-box and leucine-rich repeat protein 8, or F-box protein FBL8, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. 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: 438893  Cd Length: 35  Bit Score: 35.41  E-value: 2.78e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1571052967   4 SLPLEMLTYILSFLPLSDQKEASLVSRTWYCAA 36
Cdd:cd22121     2 ALPEEILVHIFRHLSLRDRYAAAQVCKHWREAA 34
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 3-33 3.16e-03

F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called FBX42, or just one F-box and Kelch domain-containing protein (JFK), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It specifically recognizes p53/TP53, promoting its ubiquitination and degradation. FBXO42 is also involved in the ubiquitin-proteasome system that may play a role in the pathogenesis of Parkinson's disease (PD). 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: 438882  Cd Length: 38  Bit Score: 35.39  E-value: 3.16e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1571052967   3 DSLPLEMLTYILSFL-PLSDQKEASLVSRTWY 33
Cdd:cd22110     2 NDLPEEILEYILSYLsPYGDLKSAALVCKRWH 33
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 227-338 5.58e-03

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: 39.00  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052967 227 TLRALDLSGTGLPPEALQALGQV--TGLKLEELYLhSCRDLSSEAVTILC---RQQPGLTSLDLSGcSDLTDGALLAVSR 301
Cdd:COG5238   237 SLTTLDLSNNQIGDEGVIALAEAlkNNTTVETLYL-SGNQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDEGAIALAE 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1571052967 302 GLRH---LRHLSLKKlQRLTDAGC----AALGALRELQSLDMAE 338
Cdd:COG5238   315 GLQGnktLHTLNLAY-NGIGAQGAialaKALQENTTLHSLDLSD 357
 
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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