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Conserved domains on  [gi|530383594|ref|XP_005266987|]
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F-box/LRR-repeat protein 4 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 280-326 4.91e-22

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. 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: 438889  Cd Length: 47  Bit Score: 89.22  E-value: 4.91e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530383594 280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCDPLQYIHLNLQ 326
Cdd:cd22117    1 FDLLPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNLQ 47
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 394-577 5.10e-14

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: 71.59  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 394 EVISEMCPNLQALNLSSCDKLPPqAFNHIAKLCSLKRLVLYRTKVeIEDYDVIAsmIGAKCKKLRTLDLWRCKNITENGI 473
Cdd:cd09293   21 QLLRILHSGLEWLELYMCPISDP-PLDQLSNCNKLKKLILPGSKL-IDDEGLIA--LAQSCPNLQVLDLRACENITDSGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 474 AELASGCPLLEELDLGWCPTLQSST-GCFTRLAHQLPNLQKLFLtANRSVCDTDIDELACNC-TRLQQLDILGTRMVSPA 551
Cdd:cd09293   97 VALATNCPKLQTINLGRHRNGHLITdVSLSALGKNCTFLQTVGF-AGCDVTDKGVWELASGCsKSLERLSLNNCRNLTDQ 175

                        170       180
                 ....*....|....*....|....*...
gi 530383594 552 SLRKLLES--CKDLSLLDVSFCSQIDNR 577
Cdd:cd09293  176 SIPAILASnyFPNLSVLEFRGCPLITDF 203
 
Name Accession Description Interval E-value
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 280-326 4.91e-22

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. 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: 438889  Cd Length: 47  Bit Score: 89.22  E-value: 4.91e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530383594 280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCDPLQYIHLNLQ 326
Cdd:cd22117    1 FDLLPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNLQ 47
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 394-577 5.10e-14

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: 71.59  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 394 EVISEMCPNLQALNLSSCDKLPPqAFNHIAKLCSLKRLVLYRTKVeIEDYDVIAsmIGAKCKKLRTLDLWRCKNITENGI 473
Cdd:cd09293   21 QLLRILHSGLEWLELYMCPISDP-PLDQLSNCNKLKKLILPGSKL-IDDEGLIA--LAQSCPNLQVLDLRACENITDSGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 474 AELASGCPLLEELDLGWCPTLQSST-GCFTRLAHQLPNLQKLFLtANRSVCDTDIDELACNC-TRLQQLDILGTRMVSPA 551
Cdd:cd09293   97 VALATNCPKLQTINLGRHRNGHLITdVSLSALGKNCTFLQTVGF-AGCDVTDKGVWELASGCsKSLERLSLNNCRNLTDQ 175

                        170       180
                 ....*....|....*....|....*...
gi 530383594 552 SLRKLLES--CKDLSLLDVSFCSQIDNR 577
Cdd:cd09293  176 SIPAILASnyFPNLSVLEFRGCPLITDF 203
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 280-318 4.03e-07

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 46.71  E-value: 4.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530383594  280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCDPL 318
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDS 39
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
454-479 4.88e-05

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 40.47  E-value: 4.88e-05
                           10        20
                   ....*....|....*....|....*.
gi 530383594   454 CKKLRTLDLWRCKNITENGIAELASG 479
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
400-592 2.09e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 400 CPNLQALNLSSCD--KLPPQafnhIAKLCSLKRLVLYRTKVEIEDYDViasmigAKCKKLRTLDLWRCKnITEngIAELA 477
Cdd:COG4886  181 LTNLKELDLSNNQitDLPEP----LGNLTNLEELDLSGNQLTDLPEPL------ANLTNLETLDLSNNQ-LTD--LPELG 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 478 sGCPLLEELDLGWCPtlqsstgcFTRL--AHQLPNLQKLFLTANRsVCDTDIDELAcNCTRLQQLDILGTRMVSPASLRK 555
Cdd:COG4886  248 -NLTNLEELDLSNNQ--------LTDLppLANLTNLKTLDLSNNQ-LTDLKLKELE-LLLGLNSLLLLLLLLNLLELLIL 316

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530383594 556 LLESCKDLSLLDVSFCSQIDNRAVLELNASFPKVFIK 592
Cdd:COG4886  317 LLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLL 353
FBOX smart00256
A Receptor for Ubiquitination Targets;
283-310 2.00e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.26  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|....*...
gi 530383594   283 LPYELIQLILNHLTLPDLCRLAQTCKLL 310
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKW 28
 
Name Accession Description Interval E-value
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 280-326 4.91e-22

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. 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: 438889  Cd Length: 47  Bit Score: 89.22  E-value: 4.91e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530383594 280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCDPLQYIHLNLQ 326
Cdd:cd22117    1 FDLLPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNLQ 47
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 394-577 5.10e-14

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: 71.59  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 394 EVISEMCPNLQALNLSSCDKLPPqAFNHIAKLCSLKRLVLYRTKVeIEDYDVIAsmIGAKCKKLRTLDLWRCKNITENGI 473
Cdd:cd09293   21 QLLRILHSGLEWLELYMCPISDP-PLDQLSNCNKLKKLILPGSKL-IDDEGLIA--LAQSCPNLQVLDLRACENITDSGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 474 AELASGCPLLEELDLGWCPTLQSST-GCFTRLAHQLPNLQKLFLtANRSVCDTDIDELACNC-TRLQQLDILGTRMVSPA 551
Cdd:cd09293   97 VALATNCPKLQTINLGRHRNGHLITdVSLSALGKNCTFLQTVGF-AGCDVTDKGVWELASGCsKSLERLSLNNCRNLTDQ 175

                        170       180
                 ....*....|....*....|....*...
gi 530383594 552 SLRKLLES--CKDLSLLDVSFCSQIDNR 577
Cdd:cd09293  176 SIPAILASnyFPNLSVLEFRGCPLITDF 203
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 280-318 4.03e-07

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 46.71  E-value: 4.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530383594  280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCDPL 318
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDS 39
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 281-315 2.68e-06

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: 43.97  E-value: 2.68e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 530383594 281 DKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCC 315
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box_FBXO36 cd22106
F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called ...
 280-316 2.41e-05

F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called FBX36, likely functions as 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: 438878  Cd Length: 46  Bit Score: 41.79  E-value: 2.41e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 530383594 280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCD 316
Cdd:cd22106    1 LVRLPDKLLLYIISYLDLEDIARLSQTSKRFKKLCNS 37
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 280-322 4.46e-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: 40.99  E-value: 4.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530383594  280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCDPLQYIH 322
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
454-479 4.88e-05

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 40.47  E-value: 4.88e-05
                           10        20
                   ....*....|....*....|....*.
gi 530383594   454 CKKLRTLDLWRCKNITENGIAELASG 479
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
400-592 2.09e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 400 CPNLQALNLSSCD--KLPPQafnhIAKLCSLKRLVLYRTKVEIEDYDViasmigAKCKKLRTLDLWRCKnITEngIAELA 477
Cdd:COG4886  181 LTNLKELDLSNNQitDLPEP----LGNLTNLEELDLSGNQLTDLPEPL------ANLTNLETLDLSNNQ-LTD--LPELG 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383594 478 sGCPLLEELDLGWCPtlqsstgcFTRL--AHQLPNLQKLFLTANRsVCDTDIDELAcNCTRLQQLDILGTRMVSPASLRK 555
Cdd:COG4886  248 -NLTNLEELDLSNNQ--------LTDLppLANLTNLKTLDLSNNQ-LTDLKLKELE-LLLGLNSLLLLLLLLNLLELLIL 316

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530383594 556 LLESCKDLSLLDVSFCSQIDNRAVLELNASFPKVFIK 592
Cdd:COG4886  317 LLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLL 353
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
 283-309 6.22e-04

F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called FBX10, or PRMT11, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an anti-apoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. It also associates with the receptor for advanced glycation end products (RAGE) to mediate its ubiquitination and degradation. 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: 438862  Cd Length: 50  Bit Score: 37.72  E-value: 6.22e-04
                         10        20
                 ....*....|....*....|....*..
gi 530383594 283 LPYELIQLILNHLTLPDLCRLAQTCKL 309
Cdd:cd22090    5 LPLELWRLILAYLPVRDLCRCCQVCRA 31
FBOX smart00256
A Receptor for Ubiquitination Targets;
283-310 2.00e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.26  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|....*...
gi 530383594   283 LPYELIQLILNHLTLPDLCRLAQTCKLL 310
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKW 28
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
400-425 3.28e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 35.07  E-value: 3.28e-03
                           10        20
                   ....*....|....*....|....*.
gi 530383594   400 CPNLQALNLSSCDKLPPQAFNHIAKL 425
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
F-box_AtSKIP3-like cd22162
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 3 (AtSKIP3) and similar ...
 280-310 4.34e-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: 35.25  E-value: 4.34e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530383594 280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLL 310
Cdd:cd22162    1 LEDLPEDCIALILSFTSPRDVCRLSAVSKTF 31
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
 283-308 5.16e-03

F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called FBX48, is one of the paralogs of the F-box only protein 7 (FBXO7), which is the causative gene for PARK15 (also known as Parkinsonian-pyramidal disease, PPD). 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: 438885  Cd Length: 46  Bit Score: 35.37  E-value: 5.16e-03
                         10        20
                 ....*....|....*....|....*.
gi 530383594 283 LPYELIQLILNHLTLPDLCRLAQTCK 308
Cdd:cd22113    4 LPPEMSLRIFSQLDVQSLCRASQTCK 29
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
 279-308 8.18e-03

F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, also called F-box and WD-40 domain-containing protein 8, or F-box only protein 29 (FBXO29), is the substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as GORASP1, IRS1, MAP4K1/HPK1. 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: 438906  Cd Length: 48  Bit Score: 34.66  E-value: 8.18e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530383594 279 YFD-KLPYELIQLILNHLTLPDLCRLAQTCK 308
Cdd:cd22134    2 FFDiQLPRELALKIFQYLSVTDLCRCAQVSK 32
F-box_FBXO47 cd22112
F-box domain found in F-box only protein 47 (FBXO47) and similar proteins; FBXO47, also called ...
 280-313 8.35e-03

F-box domain found in F-box only protein 47 (FBXO47) and similar proteins; FBXO47, also called FBX47, functions as the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It has a potential role as a tumor-suppressor gene. 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: 438884  Cd Length: 39  Bit Score: 34.44  E-value: 8.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 530383594 280 FDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQH 313
Cdd:cd22112    1 FERLPLELFFMILQYLSVEDLSILSLTSKAMRNL 34
 
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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