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Conserved domains on  [gi|340805881|ref|NP_001230049|]
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S-phase kinase-associated protein 2 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FBXL18_LRR super family cl45131
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 14-131 2.71e-03

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.


The actual alignment was detected with superfamily member pfam19729:

Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 38.18  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805881   14 KNSNLVRLNLSGCSGFSEFALQTLLSS---CSRLDELNLSWCfdftekhvqvavAHVseTITQLNLSGYRKNLQKSDLST 90
Cdd:pfam19729 229 KFSNPFYLSFSRCTLSGGQLIQRVLNGgkdLRSLVSLNLSGC------------VHC--LLPDSLLRKAEDDIDSSIVET 294

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 340805881   91 LVRRCPNLVHLDLS-----DSVMLKNDCFQEFFQLNYLQHLSLSRC 131
Cdd:pfam19729 295 LVACCPNLRHLNLSaahhhSSEGLGGHLCALLARLKHLRSLSLPVC 340
 
Name Accession Description Interval E-value
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 14-131 2.71e-03

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: 38.18  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805881   14 KNSNLVRLNLSGCSGFSEFALQTLLSS---CSRLDELNLSWCfdftekhvqvavAHVseTITQLNLSGYRKNLQKSDLST 90
Cdd:pfam19729 229 KFSNPFYLSFSRCTLSGGQLIQRVLNGgkdLRSLVSLNLSGC------------VHC--LLPDSLLRKAEDDIDSSIVET 294

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 340805881   91 LVRRCPNLVHLDLS-----DSVMLKNDCFQEFFQLNYLQHLSLSRC 131
Cdd:pfam19729 295 LVACCPNLRHLNLSaahhhSSEGLGGHLCALLARLKHLRSLSLPVC 340
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 17-131 7.88e-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: 36.15  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805881  17 NLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVqVAVAHVSETITQLNLSGYRKNLQKSDLS--TLVRR 94
Cdd:cd09293   53 KLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRHRNGHLITDVSlsALGKN 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 340805881  95 CPNLVHLDL-----SDSVM--LKNDCFQEffqlnyLQHLSLSRC 131
Cdd:cd09293  132 CTFLQTVGFagcdvTDKGVweLASGCSKS------LERLSLNNC 169
 
Name Accession Description Interval E-value
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 14-131 2.71e-03

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: 38.18  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805881   14 KNSNLVRLNLSGCSGFSEFALQTLLSS---CSRLDELNLSWCfdftekhvqvavAHVseTITQLNLSGYRKNLQKSDLST 90
Cdd:pfam19729 229 KFSNPFYLSFSRCTLSGGQLIQRVLNGgkdLRSLVSLNLSGC------------VHC--LLPDSLLRKAEDDIDSSIVET 294

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 340805881   91 LVRRCPNLVHLDLS-----DSVMLKNDCFQEFFQLNYLQHLSLSRC 131
Cdd:pfam19729 295 LVACCPNLRHLNLSaahhhSSEGLGGHLCALLARLKHLRSLSLPVC 340
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 17-131 7.88e-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: 36.15  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805881  17 NLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVqVAVAHVSETITQLNLSGYRKNLQKSDLS--TLVRR 94
Cdd:cd09293   53 KLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRHRNGHLITDVSlsALGKN 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 340805881  95 CPNLVHLDL-----SDSVM--LKNDCFQEffqlnyLQHLSLSRC 131
Cdd:cd09293  132 CTFLQTVGFagcdvTDKGVweLASGCSKS------LERLSLNNC 169
 
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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