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Conserved domains on  [gi|113194952|gb|ABI31287|]
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jetlag, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 41-84 2.15e-11

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 57.90  E-value: 2.15e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 113194952  41 LFDVCWDDVLIPQVAVYLSLKDLFNLRCCSRTAQRFVEAALEKR 84
Cdd:cd22126    1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFSKL 44
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 96-280 2.22e-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: 59.65  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952  96 NIDVAFRVLarcCQRLEVLHLACCRWLTDELLLPLLANNKKRLwavNLNECVNITALSLQPIIVECKELRVLKLSKCQWL 175
Cdd:cd09293   18 NISQLLRIL---HSGLEWLELYMCPISDPPLDQLSNCNKLKKL---ILPGSKLIDDEGLIALAQSCPNLQVLDLRACENI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952 176 TTGAVDALTLHQSKLVEFDISY---CGAIGERCLIIFFRKLNKLTVLSLANTpSVTDQVLIQIGNYC-RELEHINVIGCA 251
Cdd:cd09293   92 TDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCR 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 113194952 252 AISDYGVHAL--TSSCPLLQSLMVQRCPLVT 280
Cdd:cd09293  171 NLTDQSIPAIlaSNYFPNLSVLEFRGCPLIT 201
 
Name Accession Description Interval E-value
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 41-84 2.15e-11

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 57.90  E-value: 2.15e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 113194952  41 LFDVCWDDVLIPQVAVYLSLKDLFNLRCCSRTAQRFVEAALEKR 84
Cdd:cd22126    1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFSKL 44
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 96-280 2.22e-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: 59.65  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952  96 NIDVAFRVLarcCQRLEVLHLACCRWLTDELLLPLLANNKKRLwavNLNECVNITALSLQPIIVECKELRVLKLSKCQWL 175
Cdd:cd09293   18 NISQLLRIL---HSGLEWLELYMCPISDPPLDQLSNCNKLKKL---ILPGSKLIDDEGLIALAQSCPNLQVLDLRACENI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952 176 TTGAVDALTLHQSKLVEFDISY---CGAIGERCLIIFFRKLNKLTVLSLANTpSVTDQVLIQIGNYC-RELEHINVIGCA 251
Cdd:cd09293   92 TDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCR 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 113194952 252 AISDYGVHAL--TSSCPLLQSLMVQRCPLVT 280
Cdd:cd09293  171 NLTDQSIPAIlaSNYFPNLSVLEFRGCPLIT 201
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
79-224 5.55e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 37.99  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952  79 AALEKRQELHLSGNNTKNIDVAFRVLarccQRLEVLHLACCRwLTDellLPLLANNKKRLWAVNLNECvNITALSLQpiI 158
Cdd:COG4886  133 ANLTNLKELDLSNNQLTDLPEPLGNL----TNLKSLDLSNNQ-LTD---LPEELGNLTNLKELDLSNN-QITDLPEP--L 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113194952 159 VECKELRVLKLSKCQwLTT--GAVDALTlhqsKLVEFDISYCgAIGErclIIFFRKLNKLTVLSLANT 224
Cdd:COG4886  202 GNLTNLEELDLSGNQ-LTDlpEPLANLT----NLETLDLSNN-QLTD---LPELGNLTNLEELDLSNN 260
 
Name Accession Description Interval E-value
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 41-84 2.15e-11

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 57.90  E-value: 2.15e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 113194952  41 LFDVCWDDVLIPQVAVYLSLKDLFNLRCCSRTAQRFVEAALEKR 84
Cdd:cd22126    1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFSKL 44
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 96-280 2.22e-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: 59.65  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952  96 NIDVAFRVLarcCQRLEVLHLACCRWLTDELLLPLLANNKKRLwavNLNECVNITALSLQPIIVECKELRVLKLSKCQWL 175
Cdd:cd09293   18 NISQLLRIL---HSGLEWLELYMCPISDPPLDQLSNCNKLKKL---ILPGSKLIDDEGLIALAQSCPNLQVLDLRACENI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952 176 TTGAVDALTLHQSKLVEFDISY---CGAIGERCLIIFFRKLNKLTVLSLANTpSVTDQVLIQIGNYC-RELEHINVIGCA 251
Cdd:cd09293   92 TDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCR 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 113194952 252 AISDYGVHAL--TSSCPLLQSLMVQRCPLVT 280
Cdd:cd09293  171 NLTDQSIPAIlaSNYFPNLSVLEFRGCPLIT 201
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 213-287 8.80e-08

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: 51.94  E-value: 8.80e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113194952 213 LNKLTVLSLANTPSVTDQVLIQIGNYCRELEHINVIGCAAISDYGVHALTSSCPLLQSLMVQR---CPLVTERVLAPL 287
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSAL 128
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
79-224 5.55e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 37.99  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113194952  79 AALEKRQELHLSGNNTKNIDVAFRVLarccQRLEVLHLACCRwLTDellLPLLANNKKRLWAVNLNECvNITALSLQpiI 158
Cdd:COG4886  133 ANLTNLKELDLSNNQLTDLPEPLGNL----TNLKSLDLSNNQ-LTD---LPEELGNLTNLKELDLSNN-QITDLPEP--L 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113194952 159 VECKELRVLKLSKCQwLTT--GAVDALTlhqsKLVEFDISYCgAIGErclIIFFRKLNKLTVLSLANT 224
Cdd:COG4886  202 GNLTNLEELDLSGNQ-LTDlpEPLANLT----NLETLDLSNN-QLTD---LPELGNLTNLEELDLSNN 260
 
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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