NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|525342655|ref|NP_036294|]
View 

F-box/LRR-repeat protein 6 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
112-158 7.20e-17

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), 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: 438891  Cd Length: 47  Bit Score: 74.21  E-value: 7.20e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342655 112 GDRIPLEILVQIFGLLVAADGPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22119    1 GQRLPPEILVKIFQFAVATEGAVPLLCRLSRVCRLWREVALDPSLWT 47
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
185-398 1.88e-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.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 55.03  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 185 LEWLMPNRFSQLQRLTLIHWKSQVHPVLKLVgeCCPRLTFLKLSGCHGVTADALVMLAKACCQLHSLDLQH-SMVESTAV 263
Cdd:cd09293   19 ISQLLRILHSGLEWLELYMCPISDPPLDQLS--NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 264 VSfleeagsrmrklwltyssqttailgalLGSCCPQLQVLEVSTGINRNSIPlQLPVEALQKGCPQLQVLRLLNL----- 338
Cdd:cd09293   97 VA---------------------------LATNCPKLQTINLGRHRNGHLIT-DVSLSALGKNCTFLQTVGFAGCdvtdk 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525342655 339 -MWlpkppgrGVAPGPGfPSLEELCLASstCNFVSNEVLGRLLHGS--PNLRLLDLRGCARIT 398
Cdd:cd09293  149 gVW-------ELASGCS-KSLERLSLNN--CRNLTDQSIPAILASNyfPNLSVLEFRGCPLIT 201
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
357-508 4.08e-05

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: 45.01  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 357 SLEELCLASstCNFVSNEVLGRLLHGSPNLRLLDLRGCARITPAGLQDLP--CRELEQLHLGLYGTSDRLTlakEGSPFL 434
Cdd:cd09293   53 KLKKLILPG--SKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtnCPKLQTINLGRHRNGHLIT---DVSLSA 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525342655 435 TQKWCHTLRELDLSGQGFSEKDLEQalaafLSTPGGSHPALCSLNlRGTRVTPSTVSSVI--SGCPGLLYLNLESC 508
Cdd:cd09293  128 LGKNCTFLQTVGFAGCDVTDKGVWE-----LASGCSKSLERLSLN-NCRNLTDQSIPAILasNYFPNLSVLEFRGC 197
 
Name Accession Description Interval E-value
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
112-158 7.20e-17

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), 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: 438891  Cd Length: 47  Bit Score: 74.21  E-value: 7.20e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342655 112 GDRIPLEILVQIFGLLVAADGPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22119    1 GQRLPPEILVKIFQFAVATEGAVPLLCRLSRVCRLWREVALDPSLWT 47
F-box-like pfam12937
F-box-like; This is an F-box-like family.
113-160 4.07e-10

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 55.18  E-value: 4.07e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 525342655  113 DRIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAASQPALWHTV 160
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKD-----LLRLALVCRRWRELASDDSLWRRL 44
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
185-398 1.88e-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: 55.03  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 185 LEWLMPNRFSQLQRLTLIHWKSQVHPVLKLVgeCCPRLTFLKLSGCHGVTADALVMLAKACCQLHSLDLQH-SMVESTAV 263
Cdd:cd09293   19 ISQLLRILHSGLEWLELYMCPISDPPLDQLS--NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 264 VSfleeagsrmrklwltyssqttailgalLGSCCPQLQVLEVSTGINRNSIPlQLPVEALQKGCPQLQVLRLLNL----- 338
Cdd:cd09293   97 VA---------------------------LATNCPKLQTINLGRHRNGHLIT-DVSLSALGKNCTFLQTVGFAGCdvtdk 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525342655 339 -MWlpkppgrGVAPGPGfPSLEELCLASstCNFVSNEVLGRLLHGS--PNLRLLDLRGCARIT 398
Cdd:cd09293  149 gVW-------ELASGCS-KSLERLSLNN--CRNLTDQSIPAILASNyfPNLSVLEFRGCPLIT 201
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
357-508 4.08e-05

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: 45.01  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 357 SLEELCLASstCNFVSNEVLGRLLHGSPNLRLLDLRGCARITPAGLQDLP--CRELEQLHLGLYGTSDRLTlakEGSPFL 434
Cdd:cd09293   53 KLKKLILPG--SKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtnCPKLQTINLGRHRNGHLIT---DVSLSA 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525342655 435 TQKWCHTLRELDLSGQGFSEKDLEQalaafLSTPGGSHPALCSLNlRGTRVTPSTVSSVI--SGCPGLLYLNLESC 508
Cdd:cd09293  128 LGKNCTFLQTVGFAGCDVTDKGVWE-----LASGCSKSLERLSLN-NCRNLTDQSIPAILasNYFPNLSVLEFRGC 197
 
Name Accession Description Interval E-value
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
112-158 7.20e-17

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), 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: 438891  Cd Length: 47  Bit Score: 74.21  E-value: 7.20e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342655 112 GDRIPLEILVQIFGLLVAADGPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22119    1 GQRLPPEILVKIFQFAVATEGAVPLLCRLSRVCRLWREVALDPSLWT 47
F-box-like pfam12937
F-box-like; This is an F-box-like family.
113-160 4.07e-10

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 55.18  E-value: 4.07e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 525342655  113 DRIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAASQPALWHTV 160
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKD-----LLRLALVCRRWRELASDDSLWRRL 44
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
185-398 1.88e-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: 55.03  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 185 LEWLMPNRFSQLQRLTLIHWKSQVHPVLKLVgeCCPRLTFLKLSGCHGVTADALVMLAKACCQLHSLDLQH-SMVESTAV 263
Cdd:cd09293   19 ISQLLRILHSGLEWLELYMCPISDPPLDQLS--NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 264 VSfleeagsrmrklwltyssqttailgalLGSCCPQLQVLEVSTGINRNSIPlQLPVEALQKGCPQLQVLRLLNL----- 338
Cdd:cd09293   97 VA---------------------------LATNCPKLQTINLGRHRNGHLIT-DVSLSALGKNCTFLQTVGFAGCdvtdk 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525342655 339 -MWlpkppgrGVAPGPGfPSLEELCLASstCNFVSNEVLGRLLHGS--PNLRLLDLRGCARIT 398
Cdd:cd09293  149 gVW-------ELASGCS-KSLERLSLNN--CRNLTDQSIPAILASNyfPNLSVLEFRGCPLIT 201
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
113-163 3.62e-06

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: 44.17  E-value: 3.62e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525342655 113 DRIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAASQPALWHTVTLS 163
Cdd:cd22104    2 ANLPSVVLVHIFSYLPPRD-----RLRASSTCRRWREALFHPSLWRSLRLH 47
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
113-160 3.80e-05

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, 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 Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. 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: 438892  Cd Length: 44  Bit Score: 41.22  E-value: 3.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 525342655 113 DRIPLEILVQIFGLLvaadgPMPFLGRAARVCRRWQEAASQPALWHTV 160
Cdd:cd22120    2 DRLPDDVILQIFSHL-----PTNQLCRCARVCRRWYNLAWDPRLWTTI 44
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
113-159 3.86e-05

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), 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, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. 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: 438863  Cd Length: 45  Bit Score: 40.87  E-value: 3.86e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342655 113 DRIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAASQPALWHT 159
Cdd:cd22091    2 EELPDEVLLKIFSYLLEQD-----LCRAAQVCKRFNTLANDPELWKR 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
357-508 4.08e-05

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: 45.01  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342655 357 SLEELCLASstCNFVSNEVLGRLLHGSPNLRLLDLRGCARITPAGLQDLP--CRELEQLHLGLYGTSDRLTlakEGSPFL 434
Cdd:cd09293   53 KLKKLILPG--SKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtnCPKLQTINLGRHRNGHLIT---DVSLSA 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525342655 435 TQKWCHTLRELDLSGQGFSEKDLEQalaafLSTPGGSHPALCSLNlRGTRVTPSTVSSVI--SGCPGLLYLNLESC 508
Cdd:cd09293  128 LGKNCTFLQTVGFAGCDVTDKGVWE-----LASGCSKSLERLSLN-NCRNLTDQSIPAILasNYFPNLSVLEFRGC 197
F-box_FBXL14 cd22125
F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also ...
118-157 8.40e-05

F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also called F-box and leucine-rich repeat protein 14, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin-protein ligase complex, which acts by mediating ubiquitination and subsequent degradation of SNAIL1. 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: 438897  Cd Length: 41  Bit Score: 40.15  E-value: 8.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 525342655 118 EILVQIFGLLVAADgpmpfLGRAARVCRRWQEAASQPALW 157
Cdd:cd22125    6 EILAMIFSYLDVRD-----KGRAAQVCTAWRDAAYHKSVW 40
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
211-277 9.45e-05

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 44.68  E-value: 9.45e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525342655 211 VLKLVGECCPRLTFLkLSGCHG--VTADALVMLAKACCQLHSLDLQHSMVESTAVVSFLEEAGSRMRKL 277
Cdd:cd23951  246 VLGRVGQHCPRLVEL-VVCANGnsPIDEELIRIAKNCKQLSSLGLGECEVSCSALVEFAKLCGPRLTEL 313
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
113-152 1.30e-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.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 39.35  E-value: 1.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 525342655 113 DRIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAAS 152
Cdd:cd09917    1 SDLPDEILLKILSYLDPRD-----LLRLSLVCKRWRELAS 35
F-box_AtSKIP5-like cd22163
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar ...
120-161 4.00e-04

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar proteins; AtSKIP5, also called F-box protein SKIP5, is a component of SCF (SKP1-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1. 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: 438934  Cd Length: 46  Bit Score: 38.10  E-value: 4.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 525342655 120 LVQIFGLLvaadGPMPFLGRAARVCRRWQEAASQPALWHTVT 161
Cdd:cd22163    9 LMHIFSFL----TPLPDRFNAARVCKRWRALALDPRSWLRVK 46
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
113-160 8.71e-04

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. 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: 438922  Cd Length: 44  Bit Score: 37.30  E-value: 8.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 525342655 113 DRIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAASQPALWHTV 160
Cdd:cd22151    1 RKLPDDLLQEIFKRLDPKS-----LARAACVCRRWRAAARSESLWENA 43
F-box_FBXL3 cd22178
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also ...
111-157 1.23e-03

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also called F-box and leucine-rich repeat protein 3A, or F-box/LRR-repeat protein 3A, is the substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex that mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2, and thus, is involved in circadian rhythm function. It plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. 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: 438949  Cd Length: 43  Bit Score: 36.80  E-value: 1.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 525342655 111 WGDrIPLEILVQIFGLLvaadgpmPFLGRA--ARVCRRWQEAASQPALW 157
Cdd:cd22178    3 WGN-LLQDIILQIFQYL-------PLLDRAhaSQVCRNWNQVFHMPDLW 43
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
114-152 1.92e-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: 35.80  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 525342655 114 RIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAAS 152
Cdd:cd22121    2 ALPEEILVHIFRHLSLRD-----RYAAAQVCKHWREAAL 35
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
118-158 6.50e-03

F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and similar proteins; DmSKP2 is a Drosophila F-box protein that regulates cell proliferation by targeting Dacapo (Dap) for ubiquitination and proteasome-mediated degradation. It plays a role in maintaining diploidy of mitotic cells during development. 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: 438920  Cd Length: 43  Bit Score: 34.66  E-value: 6.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 525342655 118 EILVQIFGLLvaadgPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22149    7 EIILSIFKWL-----PKKTLARCARVCRRWKRLCFDESLWR 42
 
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