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Conserved domains on  [gi|1154884858|ref|NP_001336249|]
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F-box/LRR-repeat protein 2 isoform 4 [Homo sapiens]

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 ...
 63-293 6.13e-27

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: 106.26  E-value: 6.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858  63 QITKDGIEALVRG-CRGLKALLLRGCTQLeDEALKHIQNyCHELVSLNLQSCSRITDEGVVQICRGCHRLQALCLSGCSN 141
Cdd:cd09293    13 QITQSNISQLLRIlHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 142 LTDASLTALGLNCPRLQILEAAR---CSHLTDAGFTLLARNCHELEKMDLEECiLITDSTLIQLSIHCpklqalvslsfs 218
Cdd:cd09293    91 ITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGC------------ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154884858 219 diihllkmkepSHHNKKLfgfsfckSLSHCELITDDGILHLSNSTCgHERLRVLELDNCLLITDVALEHLENCRG 293
Cdd:cd09293   158 -----------SKSLERL-------SLNNCRNLTDQSIPAILASNY-FPNLSVLEFRGCPLITDFSRIILFKLWQ 213
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 63-293 6.13e-27

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: 106.26  E-value: 6.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858  63 QITKDGIEALVRG-CRGLKALLLRGCTQLeDEALKHIQNyCHELVSLNLQSCSRITDEGVVQICRGCHRLQALCLSGCSN 141
Cdd:cd09293    13 QITQSNISQLLRIlHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 142 LTDASLTALGLNCPRLQILEAAR---CSHLTDAGFTLLARNCHELEKMDLEECiLITDSTLIQLSIHCpklqalvslsfs 218
Cdd:cd09293    91 ITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGC------------ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154884858 219 diihllkmkepSHHNKKLfgfsfckSLSHCELITDDGILHLSNSTCgHERLRVLELDNCLLITDVALEHLENCRG 293
Cdd:cd09293   158 -----------SKSLERL-------SLNNCRNLTDQSIPAILASNY-FPNLSVLEFRGCPLITDFSRIILFKLWQ 213
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-312 4.59e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 38.76  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858  24 CSKLKHLDLTSC-VSITNSSLKGisegCRNLEYLNLSWCdQITkdGIEALVRGCRGLKALLLRGcTQLED--EALKHIQN 100
Cdd:COG4886   135 LTNLKELDLSNNqLTDLPEPLGN----LTNLKSLDLSNN-QLT--DLPEELGNLTNLKELDLSN-NQITDlpEPLGNLTN 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 101 ycheLVSLNLqSCSRITDEGVVQicRGCHRLQALCLSGCsNLTDasLTALGlNCPRLQILEAARCsHLTDAGFTLlarNC 180
Cdd:COG4886   207 ----LEELDL-SGNQLTDLPEPL--ANLTNLETLDLSNN-QLTD--LPELG-NLTNLEELDLSNN-QLTDLPPLA---NL 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 181 HELEKMDLEECiLITDSTLIQL-SIHCPKLQALVSLSFSDIIHLLKMKEPSHHNKKLFGFSFCKSLSHCELITDDGILHL 259
Cdd:COG4886   272 TNLKTLDLSNN-QLTDLKLKELeLLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1154884858 260 SNSTCGHERLRVLELDNCLLITDVALEHLENCRGLERLELYDCQQVTRAGIKR 312
Cdd:COG4886   351 TLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLL 403
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
50-75 8.66e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 33.53  E-value: 8.66e-03
                           10        20
                   ....*....|....*....|....*.
gi 1154884858   50 CRNLEYLNLSWCDQITKDGIEALVRG 75
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 63-293 6.13e-27

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: 106.26  E-value: 6.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858  63 QITKDGIEALVRG-CRGLKALLLRGCTQLeDEALKHIQNyCHELVSLNLQSCSRITDEGVVQICRGCHRLQALCLSGCSN 141
Cdd:cd09293    13 QITQSNISQLLRIlHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 142 LTDASLTALGLNCPRLQILEAAR---CSHLTDAGFTLLARNCHELEKMDLEECiLITDSTLIQLSIHCpklqalvslsfs 218
Cdd:cd09293    91 ITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGC------------ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154884858 219 diihllkmkepSHHNKKLfgfsfckSLSHCELITDDGILHLSNSTCgHERLRVLELDNCLLITDVALEHLENCRG 293
Cdd:cd09293   158 -----------SKSLERL-------SLNNCRNLTDQSIPAILASNY-FPNLSVLEFRGCPLITDFSRIILFKLWQ 213
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 23-170 2.29e-22

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: 93.55  E-value: 2.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858  23 FCSKLKHLDLTSCVSITNSSLKGISEGCRNLEYLNLSWCDQITKDGIEALVRGCRGLKALLL---RGCTQLEDEALKHIQ 99
Cdd:cd09293    50 NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALG 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154884858 100 NYCHELVSLNLQSCsRITDEGVVQICRGC-HRLQALCLSGCSNLTDASLTAL--GLNCPRLQILEAARCSHLTD 170
Cdd:cd09293   130 KNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 88-310 3.21e-15

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: 73.90  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858  88 TQLEDEALKHIQnyCHELVSLNLQSCSRITDEGVVQICrgCHRLQALCLSGCSNLTDASLTALGLNCPRLQILEAARCSH 167
Cdd:cd09293    15 TQSNISQLLRIL--HSGLEWLELYMCPISDPPLDQLSN--CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 168 LTDAGFTLLARNCHELEKMDL---EECILITDSTLIQLSIHCPKLQALvslsfsdiihllkmkepshhnkklfGFSFCKs 244
Cdd:cd09293    91 ITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGKNCTFLQTV-------------------------GFAGCD- 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154884858 245 lshcelITDDGILHLSnSTCGHErlrvleldncllitdvalehlencrgLERLELYDCQQVTRAGI 310
Cdd:cd09293   145 ------VTDKGVWELA-SGCSKS--------------------------LERLSLNNCRNLTDQSI 177
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-312 4.59e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 38.76  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858  24 CSKLKHLDLTSC-VSITNSSLKGisegCRNLEYLNLSWCdQITkdGIEALVRGCRGLKALLLRGcTQLED--EALKHIQN 100
Cdd:COG4886   135 LTNLKELDLSNNqLTDLPEPLGN----LTNLKSLDLSNN-QLT--DLPEELGNLTNLKELDLSN-NQITDlpEPLGNLTN 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 101 ycheLVSLNLqSCSRITDEGVVQicRGCHRLQALCLSGCsNLTDasLTALGlNCPRLQILEAARCsHLTDAGFTLlarNC 180
Cdd:COG4886   207 ----LEELDL-SGNQLTDLPEPL--ANLTNLETLDLSNN-QLTD--LPELG-NLTNLEELDLSNN-QLTDLPPLA---NL 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154884858 181 HELEKMDLEECiLITDSTLIQL-SIHCPKLQALVSLSFSDIIHLLKMKEPSHHNKKLFGFSFCKSLSHCELITDDGILHL 259
Cdd:COG4886   272 TNLKTLDLSNN-QLTDLKLKELeLLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1154884858 260 SNSTCGHERLRVLELDNCLLITDVALEHLENCRGLERLELYDCQQVTRAGIKR 312
Cdd:COG4886   351 TLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLL 403
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
50-75 8.66e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 33.53  E-value: 8.66e-03
                           10        20
                   ....*....|....*....|....*.
gi 1154884858   50 CRNLEYLNLSWCDQITKDGIEALVRG 75
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
 
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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