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Conserved domains on  [gi|31711938|gb|AAP68325|]
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At5g67250 [Arabidopsis thaliana]

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 ...
311-416 2.32e-11

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: 63.50  E-value: 2.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 311 RCKLLRKLHIDGWRTnrIGDEGLLSVAKHCLNLQELVLIGV-NATHMSLAAIASNCEKLERLAL---CGSGTIGDTEIAC 386
Cdd:cd09293  50 NCNKLKKLILPGSKL--IDDEGLIALAQSCPNLQVLDLRACeNITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSA 127
                        90       100       110
                ....*....|....*....|....*....|
gi 31711938 387 IARKCGALRKFCIKGCPVSDRGIEALAVGC 416
Cdd:cd09293 128 LGKNCTFLQTVGFAGCDVTDKGVWELASGC 157
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
44-81 5.17e-11

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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: 438930  Cd Length: 40  Bit Score: 57.47  E-value: 5.17e-11
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 31711938  44 GDLPDECLAHVFQFLG-AGDRKRCSLVCKRWLLVDGQSR 81
Cdd:cd22159   2 DLLPDEILELIFSYLSdPWDRNSCSLVCKRWYRLERATR 40
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
82-295 1.32e-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: 52.33  E-value: 1.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938  82 HRLSlDAKDEISSFLTSMfnRFDSVTKLALR-CDRksvslSDEALAMISvRCLNLTRVKLRGCREITDLGMEDFAKNCKN 160
Cdd:cd09293   9 HKLG-QITQSNISQLLRI--LHSGLEWLELYmCPI-----SDPPLDQLS-NCNKLKKLILPGSKLIDDEGLIALAQSCPN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 161 LKKLSV-GSCNFGAKGVNAMLEHCKLLEELSVKRLRGIHeaaeLIhlpddaSSSSLRSiclkelvngqvfepLLATTRTL 239
Cdd:cd09293  80 LQVLDLrACENITDSGIVALATNCPKLQTINLGRHRNGH----LI------TDVSLSA--------------LGKNCTFL 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31711938 240 KTLKIIRCLGDwDKVLQMIANGKS-SLSEIHLER-LQVSDIGLSAISKCSNVETLHIV 295
Cdd:cd09293 136 QTVGFAGCDVT-DKGVWELASGCSkSLERLSLNNcRNLTDQSIPAILASNYFPNLSVL 192
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
311-416 2.32e-11

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: 63.50  E-value: 2.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 311 RCKLLRKLHIDGWRTnrIGDEGLLSVAKHCLNLQELVLIGV-NATHMSLAAIASNCEKLERLAL---CGSGTIGDTEIAC 386
Cdd:cd09293  50 NCNKLKKLILPGSKL--IDDEGLIALAQSCPNLQVLDLRACeNITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSA 127
                        90       100       110
                ....*....|....*....|....*....|
gi 31711938 387 IARKCGALRKFCIKGCPVSDRGIEALAVGC 416
Cdd:cd09293 128 LGKNCTFLQTVGFAGCDVTDKGVWELASGC 157
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
44-81 5.17e-11

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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: 438930  Cd Length: 40  Bit Score: 57.47  E-value: 5.17e-11
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 31711938  44 GDLPDECLAHVFQFLG-AGDRKRCSLVCKRWLLVDGQSR 81
Cdd:cd22159   2 DLLPDEILELIFSYLSdPWDRNSCSLVCKRWYRLERATR 40
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
82-295 1.32e-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: 52.33  E-value: 1.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938  82 HRLSlDAKDEISSFLTSMfnRFDSVTKLALR-CDRksvslSDEALAMISvRCLNLTRVKLRGCREITDLGMEDFAKNCKN 160
Cdd:cd09293   9 HKLG-QITQSNISQLLRI--LHSGLEWLELYmCPI-----SDPPLDQLS-NCNKLKKLILPGSKLIDDEGLIALAQSCPN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 161 LKKLSV-GSCNFGAKGVNAMLEHCKLLEELSVKRLRGIHeaaeLIhlpddaSSSSLRSiclkelvngqvfepLLATTRTL 239
Cdd:cd09293  80 LQVLDLrACENITDSGIVALATNCPKLQTINLGRHRNGH----LI------TDVSLSA--------------LGKNCTFL 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31711938 240 KTLKIIRCLGDwDKVLQMIANGKS-SLSEIHLER-LQVSDIGLSAISKCSNVETLHIV 295
Cdd:cd09293 136 QTVGFAGCDVT-DKGVWELASGCSkSLERLSLNNcRNLTDQSIPAILASNYFPNLSVL 192
F-box-like pfam12937
F-box-like; This is an F-box-like family.
45-73 1.09e-06

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 45.17  E-value: 1.09e-06
                          10        20
                  ....*....|....*....|....*....
gi 31711938    45 DLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:pfam12937   3 SLPDEILLQIFSYLDPKDLLRLALVCRRW 31
FBOX smart00256
A Receptor for Ubiquitination Targets;
46-73 3.55e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 38.19  E-value: 3.55e-04
                           10        20
                   ....*....|....*....|....*...
gi 31711938     46 LPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKW 28
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
311-416 2.32e-11

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: 63.50  E-value: 2.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 311 RCKLLRKLHIDGWRTnrIGDEGLLSVAKHCLNLQELVLIGV-NATHMSLAAIASNCEKLERLAL---CGSGTIGDTEIAC 386
Cdd:cd09293  50 NCNKLKKLILPGSKL--IDDEGLIALAQSCPNLQVLDLRACeNITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSA 127
                        90       100       110
                ....*....|....*....|....*....|
gi 31711938 387 IARKCGALRKFCIKGCPVSDRGIEALAVGC 416
Cdd:cd09293 128 LGKNCTFLQTVGFAGCDVTDKGVWELASGC 157
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
44-81 5.17e-11

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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: 438930  Cd Length: 40  Bit Score: 57.47  E-value: 5.17e-11
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 31711938  44 GDLPDECLAHVFQFLG-AGDRKRCSLVCKRWLLVDGQSR 81
Cdd:cd22159   2 DLLPDEILELIFSYLSdPWDRNSCSLVCKRWYRLERATR 40
F-box_FBXO39 cd22108
F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called ...
46-73 7.72e-08

F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called FBX39, likely functions as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a cancer/testis antigen from colon cancer patients by serological analysis of recombinant cDNA expression libraries (SEREX). 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: 438880  Cd Length: 44  Bit Score: 48.57  E-value: 7.72e-08
                        10        20
                ....*....|....*....|....*...
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22108   4 LPDVCLRHVFRWLGDRDRSRAALVCKRW 31
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
275-418 9.71e-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: 52.71  E-value: 9.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 275 VSDIGLSAISKCSNVETLHIVKTPECSNFGLIYVAERCKLLRklHIDGWRTNRIGDEGLLSVAKHCLNLQELVLIGVNAT 354
Cdd:cd09293  40 ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQ--VLDLRACENITDSGIVALATNCPKLQTINLGRHRNG 117
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31711938 355 HM----SLAAIASNCEKLERLALCGSGtIGDTEIACIARKCG-ALRKFCIKGCP-VSDRGIEALAV--GCPN 418
Cdd:cd09293 118 HLitdvSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRnLTDQSIPAILAsnYFPN 188
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
82-295 1.32e-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: 52.33  E-value: 1.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938  82 HRLSlDAKDEISSFLTSMfnRFDSVTKLALR-CDRksvslSDEALAMISvRCLNLTRVKLRGCREITDLGMEDFAKNCKN 160
Cdd:cd09293   9 HKLG-QITQSNISQLLRI--LHSGLEWLELYmCPI-----SDPPLDQLS-NCNKLKKLILPGSKLIDDEGLIALAQSCPN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 161 LKKLSV-GSCNFGAKGVNAMLEHCKLLEELSVKRLRGIHeaaeLIhlpddaSSSSLRSiclkelvngqvfepLLATTRTL 239
Cdd:cd09293  80 LQVLDLrACENITDSGIVALATNCPKLQTINLGRHRNGH----LI------TDVSLSA--------------LGKNCTFL 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31711938 240 KTLKIIRCLGDwDKVLQMIANGKS-SLSEIHLER-LQVSDIGLSAISKCSNVETLHIV 295
Cdd:cd09293 136 QTVGFAGCDVT-DKGVWELASGCSkSLERLSLNNcRNLTDQSIPAILASNYFPNLSVL 192
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
45-73 7.16e-07

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: 45.51  E-value: 7.16e-07
                        10        20
                ....*....|....*....|....*....
gi 31711938  45 DLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd09917   2 DLPDEILLKILSYLDPRDLLRLSLVCKRW 30
F-box-like pfam12937
F-box-like; This is an F-box-like family.
45-73 1.09e-06

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 45.17  E-value: 1.09e-06
                          10        20
                  ....*....|....*....|....*....
gi 31711938    45 DLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:pfam12937   3 SLPDEILLQIFSYLDPKDLLRLALVCRRW 31
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
45-78 3.25e-06

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: 43.86  E-value: 3.25e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 31711938  45 DLPDECLAHVFQFLG-AGDRKRCSLVCKRWL-LVDG 78
Cdd:cd22110   3 DLPEEILEYILSYLSpYGDLKSAALVCKRWHrIIKG 38
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
46-74 8.06e-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: 43.01  E-value: 8.06e-06
                        10        20
                ....*....|....*....|....*....
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRWL 74
Cdd:cd22104   4 LPSVVLVHIFSYLPPRDRLRASSTCRRWR 32
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
45-73 1.78e-05

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: 41.76  E-value: 1.78e-05
                          10        20
                  ....*....|....*....|....*....
gi 31711938    45 DLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:pfam00646   3 DLPDDLLLEILSRLDPKDLLRLSLVSKRW 31
F-box_FBXL3-like cd22116
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3), F-box/LRR-repeat protein 21 (FBXL21) ...
44-73 7.53e-05

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3), F-box/LRR-repeat protein 21 (FBXL21) 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. FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B, or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is also involved in circadian rhythm function. It plays regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. 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: 438888  Cd Length: 39  Bit Score: 40.20  E-value: 7.53e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 31711938  44 GDLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22116   3 GNLPSDIILHIFQYLPLLDRAHASLVCRLW 32
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
46-73 7.92e-05

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: 40.04  E-value: 7.92e-05
                        10        20
                ....*....|....*....|....*...
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22121   3 LPEEILVHIFRHLSLRDRYAAAQVCKHW 30
F-box_FBXL21 cd22179
F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also ...
44-73 1.30e-04

F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B (FBXL3B), or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is involved in circadian rhythm function. It regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. 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: 438950  Cd Length: 43  Bit Score: 39.51  E-value: 1.30e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 31711938  44 GDLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22179   4 GNLPHHVVLHIFQYLPLVDRARASSVCRRW 33
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
44-73 1.35e-04

F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called FBX18, or F-box DNA helicase 1 (FBH1), is a 3'-5' DNA helicase and the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks. 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: 438867  Cd Length: 48  Bit Score: 39.56  E-value: 1.35e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 31711938  44 GDLPDECLAHVFQFLGAGDRKR-CSLVCKRW 73
Cdd:cd22095   3 QQLPEELLRNIFAFLPAEDLYQnISLVCRHW 33
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
46-79 1.55e-04

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. 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: 438890  Cd Length: 41  Bit Score: 39.24  E-value: 1.55e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRW--LLVDGQ 79
Cdd:cd22118   4 LPPEIMLKIFSYLNPQDLCRCAQVCTKWsqLARDGS 39
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
46-87 3.54e-04

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, 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 involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. 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: 438886  Cd Length: 41  Bit Score: 38.16  E-value: 3.54e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRWllvdgqsrHRLSLD 87
Cdd:cd22114   4 LPDELLLGIFSCLCLPDLLKVSQVCKRW--------YRLASD 37
FBOX smart00256
A Receptor for Ubiquitination Targets;
46-73 3.55e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 38.19  E-value: 3.55e-04
                           10        20
                   ....*....|....*....|....*...
gi 31711938     46 LPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKW 28
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
45-87 3.93e-04

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. 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: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 38.36  E-value: 3.93e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 31711938  45 DLPDECLAHVFQFLGAGDRKRCSLVCKRWllvdgqsrHRLSLD 87
Cdd:cd22132   3 LLPDSLLLHIFSYLSPKDLLAAGQVCKQW--------YRVSRD 37
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
47-81 4.62e-04

F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and responses to stress. COI1 is an F-box protein that functions as the substrate-recruiting module of the Skp1-Cul1-F-box protein (SCF) ubiquitin E3 ligase complex. The role of COI1-mediated JAZ degradation in jasmonate (JA) signaling is analogous to auxin signaling through the receptor F-box protein transport inhibitor response 1 (TIR1), which promotes hormone-dependent turnover of the AUX/IAA transcriptional repressors. The crystal structure of COI1 reveals a TIR1-like overall architecture, with an N-terminal tri-helical F-box motif bound to ASK1 and a C-terminal horseshoe-shaped solenoid domain formed by 18 tandem leucine-rich repeats. This entry represents the N-terminal F-box domain which is also found in other auxin signaling f-box proteins such as AFB1, AFB2 and AFB3.


Pssm-ID: 436553  Cd Length: 42  Bit Score: 37.93  E-value: 4.62e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 31711938    47 PDECLAHVFQFL-GAGDRKRCSLVCKRWLLVDGQSR 81
Cdd:pfam18511   5 PDEVLECVLPYItSPRDRNAVSLVCKRWYRIEALTR 40
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
209-416 5.31e-04

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: 42.37  E-value: 5.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 209 DASSSSLRSIC--LKELVNGqvfepllattrTLKTLKIIRCLG----DWDKV-----LQMIANGKSSLSEIHLERLQVSD 277
Cdd:cd23951  40 DSSQESAEAACdiLSQLVNC-----------SLKTLGLMSTAKpsflDVDQSkfvsaLTVVFDHSSSLSSLAIDDTPVDD 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 278 IGLS--AISKCSNVETLHIVKTPECSNFGLIYVAERCKLLRKL--------------------------HIDGWRTN--- 326
Cdd:cd23951 109 PSLQtlASSSSDTLELLKMKSCPRVSPRGILAVADHCQHLRELslnyhllsddlllalsseehvrlehlRIDVVSENdgp 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711938 327 ----RIGDEGLLSVAKHCLNL--------------QELVLIGVNATHM---------SLAAIASNCEKLERLALCGSGTI 379
Cdd:cd23951 189 mplhQISKESWDALIKHSPDVnlvmyffvlededfDPFFRSYTPVTHLyfgrsvpkaVLGRVGQHCPRLVELVVCANGNS 268
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 31711938 380 G-DTEIACIARKCGALRKFCIKGCPVSDRGIEALAVGC 416
Cdd:cd23951 269 PiDEELIRIAKNCKQLSSLGLGECEVSCSALVEFAKLC 306
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
45-72 8.54e-04

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). 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: 438856  Cd Length: 49  Bit Score: 37.24  E-value: 8.54e-04
                        10        20
                ....*....|....*....|....*...
gi 31711938  45 DLPDECLAHVFQFLGAGDRKRCSLVCKR 72
Cdd:cd22084   3 DLPSDPLLNILSFLDYRDLISCSQVCRR 30
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
45-73 9.95e-04

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). 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: 438910  Cd Length: 45  Bit Score: 36.92  E-value: 9.95e-04
                        10        20
                ....*....|....*....|....*....
gi 31711938  45 DLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22138   3 SLPVECQLKIFSFLSEVDKCLAATVCRSW 31
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
46-73 1.64e-03

F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called FBX45, or F-box/SPRY domain-containing protein 1, functions as the substrate-recognition component of E3 ubiquitin ligase complexes. It is critical for synaptogenesis, neuronal migration, and synaptic transmission. 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: 438883  Cd Length: 36  Bit Score: 36.11  E-value: 1.64e-03
                        10        20
                ....*....|....*....|....*...
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22111   4 LPSRVLEVIFSYLDLPDLRNCSLVCKSW 31
F-box_AtSKIP3-like cd22162
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 3 (AtSKIP3) and similar ...
44-71 1.79e-03

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 3 (AtSKIP3) and similar proteins; AtSKIP3, also called F-box protein SKIP3, F-box protein PP2-B9, or protein PHLOEM PROTEIN 2-LIKE B9, 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. This subfamily also includes many other Arabidopsis thaliana protein PHLOEM PROTEIN 2-LIKE 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: 438933  Cd Length: 46  Bit Score: 36.41  E-value: 1.79e-03
                        10        20
                ....*....|....*....|....*...
gi 31711938  44 GDLPDECLAHVFQFLGAGDRKRCSLVCK 71
Cdd:cd22162   2 EDLPEDCIALILSFTSPRDVCRLSAVSK 29
F-box_FBXL3 cd22178
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also ...
44-73 2.14e-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: 36.03  E-value: 2.14e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 31711938  44 GDLPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22178   4 GNLLQDIILQIFQYLPLLDRAHASQVCRNW 33
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
46-87 3.22e-03

F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; The JHDM family includes F-box/LRR-repeat proteins FBXL10, FBXL11 and FBXL19. FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10 (FBL10), JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. FBXL11, also called KDM2A, CXXC8, F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. FBXL19, also called F-box and leucine-rich repeat protein 19, is the substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It acts as a CpG island-binding protein in mouse embryonic stem (ES) cells and has been shown to associate with the CDK-Mediator complex. It promotes H2Bub1 at the promoters of CpG island-containing genes by interacting with RNF20. 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: 438894  Cd Length: 43  Bit Score: 35.71  E-value: 3.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRWllvdgqsrHRLSLD 87
Cdd:cd22122   4 LPREVWLPVFQYLSPKDLCVCMRVCKTW--------NRWCCD 37
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
46-73 5.35e-03

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: 35.05  E-value: 5.35e-03
                        10        20
                ....*....|....*....|....*...
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22120   4 LPDDVILQIFSHLPTNQLCRCARVCRRW 31
F-box_AtSKIP5-like cd22163
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar ...
45-73 5.43e-03

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: 35.01  E-value: 5.43e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 31711938  45 DLPDECLAHVFQFLGA-GDRKRCSLVCKRW 73
Cdd:cd22163   3 DLDDDCLMHIFSFLTPlPDRFNAARVCKRW 32
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
44-72 5.59e-03

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). 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: 438911  Cd Length: 45  Bit Score: 34.91  E-value: 5.59e-03
                        10        20
                ....*....|....*....|....*....
gi 31711938  44 GDLPDECLAHVFQFLGAGDRKRCSLVCKR 72
Cdd:cd22139   2 LCLPDELWLHIFSFLSPKDLCQVALVCRR 30
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
46-73 7.32e-03

F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also called F-box and leucine-rich repeat protein 12, or F-box protein FBL12, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the polyubiquitination and proteasomal degradation of calcium/calmodulin dependent protein kinase I (CAMK1) leading to disruption of cyclin D1/CDK4 complex assembly, which results in G1 cell cycle arrest in lung epithelia. It regulates T-cell differentiation in a cell-autonomous manner. 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: 438895  Cd Length: 42  Bit Score: 34.63  E-value: 7.32e-03
                        10        20
                ....*....|....*....|....*...
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRW 73
Cdd:cd22123   4 LPENVLLEILSYLPVRDLLRISRVCKRW 31
F-box_AtARP8-like cd22156
F-box domain found in Arabidopsis thaliana actin-related protein 8 (AtARP8) and similar ...
46-79 7.78e-03

F-box domain found in Arabidopsis thaliana actin-related protein 8 (AtARP8) and similar proteins; AtARP8, also called F-box protein ARP8, is an F-box protein localized to the nucleolus in Arabidopsis. Unlike other plant nuclear actin-related proteins (ARPs), ARP8 is unique in having an F-box domain and an actin homology domain. It may play a role in nucleolar functions. 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: 438927  Cd Length: 45  Bit Score: 34.66  E-value: 7.78e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 31711938  46 LPDECLAHVFQFLGAGDRKRCSLVCKRW--LLVDGQ 79
Cdd:cd22156   5 LPEDVLMQILRLLGPKDAAKLCLVCKSWryLVSDNR 40
 
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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