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Conserved domains on  [gi|157426875|ref|NP_079239|]
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F-box/LRR-repeat protein 18 isoform 2 [Homo sapiens]

Protein Classification

F-box/LRR-repeat protein 18( domain architecture ID 17778604)

F-box/LRR-repeat protein 18 functions as the substrate-recognition component of an SCF (Skp1-cullin-F-box) E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins

CATH:  1.20.1280.50
Gene Symbol:  FBXL18
Gene Ontology:  GO:0006511|GO:0019005|GO:0005515
PubMed:  31898225|11178263|14747988|11751054
SCOP:  4001927|4003523

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 85-675 0e+00

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


:

Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 1173.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875   85 VRQLVKEIGREIQQLSMAGCYWLPGSTVEHVARCRSLVKVNLSGCHLTSLRLSKMLSALQHLRSLAIDVSPGFDASQLSS 164
Cdd:pfam19729   1 VKQLLKELANEIQQLSLSGCYWLSGSTVDQVTRCRNLVKLDLSGCRLTSLRLSKLLSSLQHLRSLAIDVNPGFDASQLSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  165 ECKATLSRVRELKQTLFTPSYGVVPCCTSLEKLLLYFEILDRTREGAILSGQLMVGQSNVPHYQNLRVFYARLAPGYINQ 244
Cdd:pfam19729  81 ECKATLSRVRELKQTLFTPSYGVVPCCTSLEKLLLYFEILDRTREGVGLSGQLMVGQSNVPHYQNLRVFYARLAPGYVNQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  245 EVVRLYLAVLSDRTPQNLHAFLISVPGSFAESG-ATKNLLDSMARNVVLDALQLPKSWLNGSSLLQHMKFNNPFYFSFSR 323
Cdd:pfam19729 161 EVLRLYLAVFSVRTPENLRAFLISVPGPFAESGpATKNLLDSMAKNVSLEALQLPRSWLNGSSLLQHLKFSNPFYLSFSR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  324 CTLSGGHLIQQVINGGKDLRSLASLNLSGCVHCLSPDSLLRKAEDDIDSSILETLVASCCNLRHLNLSAAHHHSSEGLGR 403
Cdd:pfam19729 241 CTLSGGQLIQRVLNGGKDLRSLVSLNLSGCVHCLLPDSLLRKAEDDIDSSIVETLVACCPNLRHLNLSAAHHHSSEGLGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  404 HLCQLLARLRHLRSLSLPVCSVADSAPRADRAPAQP--AMHAVPRGFGKKVRVGVQSCPSPFSGQACPQPSSVFWSLLKN 481
Cdd:pfam19729 321 HLCALLARLKHLRSLSLPVCAVADSAKTADKSPSQTdlASSAVPLGFGKKVRIGVQTYPRDSSEQASPDPTSVFWTLLKG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  482 LPFLEHLELIGSNFSSAMPRNEPAIRNSLPPCSRAQSVGDSEVAAIGQLAFLRHLTLAQLPSVLTGSGLVNIGLQCQQLR 561
Cdd:pfam19729 401 CPFLEELELIGSNFSSAMPRNEPAIRNSLPPCARAQSVGDSEVAAIGQLAFLRRLTLAQLPGILTGSGLVQIGLQCQDLQ 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  562 SLSLANLGMMGKVVYMPALSDMLKHCKRLRDLRLEQPYFSANAQFFQALSQCPSLQRLCLVSRSGTLQPDAVLAFMARCL 641
Cdd:pfam19729 481 VLSLANLGMLGKVNYMPALCEMLKHCKQLKDLRLEQPYFSANAQFFQALSHCSSLQRLCIVSRSGTFQPDAVLSFMASCL 560

                         570       580       590
                  ....*....|....*....|....*....|....
gi 157426875  642 QVVMCHLFTGESLATCKSLQQSLLRSFQAERPAL 675
Cdd:pfam19729 561 HVVMCHMFTGETLVACKNLQQSLLRSFQAERPAL 594
F-box_FBXL18 cd22128
F-box domain found in F-box/LRR-repeat protein 18 (FBXL18) and similar proteins; FBXL18, also ...
 28-71 3.42e-19

F-box domain found in F-box/LRR-repeat protein 18 (FBXL18) and similar proteins; FBXL18, also called F-box and leucine-rich repeat protein 18, is a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It promotes glioma progression by promoting K63-linked ubiquitination of Akt. It targets leucine-rich repeat kinase 2 (LRRK2) for proteasomal degradation and attenuates cell toxicity. FBXL18 also regulates apoptosis by mediating ubiquitin-dependent proteasomal degradation of the pro-apoptotic protein FBXL7 that may impact cellular processes involved in cell cycle progression. 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: 438900  Cd Length: 44  Bit Score: 81.33  E-value: 3.42e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157426875  28 LLGFSDEILLHILSHVPSTDLILNVRRTCRKLAALCLDKSLIHT 71
Cdd:cd22128    1 LTEFSDEILLNILRFVPSTDLILNVRRTCRKLATLCLDKSLIHS 44
 
Name Accession Description Interval E-value
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 85-675 0e+00

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 1173.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875   85 VRQLVKEIGREIQQLSMAGCYWLPGSTVEHVARCRSLVKVNLSGCHLTSLRLSKMLSALQHLRSLAIDVSPGFDASQLSS 164
Cdd:pfam19729   1 VKQLLKELANEIQQLSLSGCYWLSGSTVDQVTRCRNLVKLDLSGCRLTSLRLSKLLSSLQHLRSLAIDVNPGFDASQLSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  165 ECKATLSRVRELKQTLFTPSYGVVPCCTSLEKLLLYFEILDRTREGAILSGQLMVGQSNVPHYQNLRVFYARLAPGYINQ 244
Cdd:pfam19729  81 ECKATLSRVRELKQTLFTPSYGVVPCCTSLEKLLLYFEILDRTREGVGLSGQLMVGQSNVPHYQNLRVFYARLAPGYVNQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  245 EVVRLYLAVLSDRTPQNLHAFLISVPGSFAESG-ATKNLLDSMARNVVLDALQLPKSWLNGSSLLQHMKFNNPFYFSFSR 323
Cdd:pfam19729 161 EVLRLYLAVFSVRTPENLRAFLISVPGPFAESGpATKNLLDSMAKNVSLEALQLPRSWLNGSSLLQHLKFSNPFYLSFSR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  324 CTLSGGHLIQQVINGGKDLRSLASLNLSGCVHCLSPDSLLRKAEDDIDSSILETLVASCCNLRHLNLSAAHHHSSEGLGR 403
Cdd:pfam19729 241 CTLSGGQLIQRVLNGGKDLRSLVSLNLSGCVHCLLPDSLLRKAEDDIDSSIVETLVACCPNLRHLNLSAAHHHSSEGLGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  404 HLCQLLARLRHLRSLSLPVCSVADSAPRADRAPAQP--AMHAVPRGFGKKVRVGVQSCPSPFSGQACPQPSSVFWSLLKN 481
Cdd:pfam19729 321 HLCALLARLKHLRSLSLPVCAVADSAKTADKSPSQTdlASSAVPLGFGKKVRIGVQTYPRDSSEQASPDPTSVFWTLLKG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  482 LPFLEHLELIGSNFSSAMPRNEPAIRNSLPPCSRAQSVGDSEVAAIGQLAFLRHLTLAQLPSVLTGSGLVNIGLQCQQLR 561
Cdd:pfam19729 401 CPFLEELELIGSNFSSAMPRNEPAIRNSLPPCARAQSVGDSEVAAIGQLAFLRRLTLAQLPGILTGSGLVQIGLQCQDLQ 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  562 SLSLANLGMMGKVVYMPALSDMLKHCKRLRDLRLEQPYFSANAQFFQALSQCPSLQRLCLVSRSGTLQPDAVLAFMARCL 641
Cdd:pfam19729 481 VLSLANLGMLGKVNYMPALCEMLKHCKQLKDLRLEQPYFSANAQFFQALSHCSSLQRLCIVSRSGTFQPDAVLSFMASCL 560

                         570       580       590
                  ....*....|....*....|....*....|....
gi 157426875  642 QVVMCHLFTGESLATCKSLQQSLLRSFQAERPAL 675
Cdd:pfam19729 561 HVVMCHMFTGETLVACKNLQQSLLRSFQAERPAL 594
F-box_FBXL18 cd22128
F-box domain found in F-box/LRR-repeat protein 18 (FBXL18) and similar proteins; FBXL18, also ...
 28-71 3.42e-19

F-box domain found in F-box/LRR-repeat protein 18 (FBXL18) and similar proteins; FBXL18, also called F-box and leucine-rich repeat protein 18, is a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It promotes glioma progression by promoting K63-linked ubiquitination of Akt. It targets leucine-rich repeat kinase 2 (LRRK2) for proteasomal degradation and attenuates cell toxicity. FBXL18 also regulates apoptosis by mediating ubiquitin-dependent proteasomal degradation of the pro-apoptotic protein FBXL7 that may impact cellular processes involved in cell cycle progression. 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: 438900  Cd Length: 44  Bit Score: 81.33  E-value: 3.42e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157426875  28 LLGFSDEILLHILSHVPSTDLILNVRRTCRKLAALCLDKSLIHT 71
Cdd:cd22128    1 LTEFSDEILLNILRFVPSTDLILNVRRTCRKLATLCLDKSLIHS 44
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 33-68 4.27e-05

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 41.31  E-value: 4.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 157426875   33 DEILLHILSHVPSTDLiLNVRRTCRKLAALCLDKSL 68
Cdd:pfam12937   6 DEILLQIFSYLDPKDL-LRLALVCRRWRELASDDSL 40
FBOX smart00256
A Receptor for Ubiquitination Targets;
33-70 9.92e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 37.42  E-value: 9.92e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 157426875    33 DEILLHILSHVPSTDLiLNVRRTCRKLAALCLDKSLIH 70
Cdd:smart00256   3 DEILEEILSKLDPKDL-LRLRKVSRKWRSLIDSHDFWF 39
 
Name Accession Description Interval E-value
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 85-675 0e+00

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 1173.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875   85 VRQLVKEIGREIQQLSMAGCYWLPGSTVEHVARCRSLVKVNLSGCHLTSLRLSKMLSALQHLRSLAIDVSPGFDASQLSS 164
Cdd:pfam19729   1 VKQLLKELANEIQQLSLSGCYWLSGSTVDQVTRCRNLVKLDLSGCRLTSLRLSKLLSSLQHLRSLAIDVNPGFDASQLSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  165 ECKATLSRVRELKQTLFTPSYGVVPCCTSLEKLLLYFEILDRTREGAILSGQLMVGQSNVPHYQNLRVFYARLAPGYINQ 244
Cdd:pfam19729  81 ECKATLSRVRELKQTLFTPSYGVVPCCTSLEKLLLYFEILDRTREGVGLSGQLMVGQSNVPHYQNLRVFYARLAPGYVNQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  245 EVVRLYLAVLSDRTPQNLHAFLISVPGSFAESG-ATKNLLDSMARNVVLDALQLPKSWLNGSSLLQHMKFNNPFYFSFSR 323
Cdd:pfam19729 161 EVLRLYLAVFSVRTPENLRAFLISVPGPFAESGpATKNLLDSMAKNVSLEALQLPRSWLNGSSLLQHLKFSNPFYLSFSR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  324 CTLSGGHLIQQVINGGKDLRSLASLNLSGCVHCLSPDSLLRKAEDDIDSSILETLVASCCNLRHLNLSAAHHHSSEGLGR 403
Cdd:pfam19729 241 CTLSGGQLIQRVLNGGKDLRSLVSLNLSGCVHCLLPDSLLRKAEDDIDSSIVETLVACCPNLRHLNLSAAHHHSSEGLGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  404 HLCQLLARLRHLRSLSLPVCSVADSAPRADRAPAQP--AMHAVPRGFGKKVRVGVQSCPSPFSGQACPQPSSVFWSLLKN 481
Cdd:pfam19729 321 HLCALLARLKHLRSLSLPVCAVADSAKTADKSPSQTdlASSAVPLGFGKKVRIGVQTYPRDSSEQASPDPTSVFWTLLKG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  482 LPFLEHLELIGSNFSSAMPRNEPAIRNSLPPCSRAQSVGDSEVAAIGQLAFLRHLTLAQLPSVLTGSGLVNIGLQCQQLR 561
Cdd:pfam19729 401 CPFLEELELIGSNFSSAMPRNEPAIRNSLPPCARAQSVGDSEVAAIGQLAFLRRLTLAQLPGILTGSGLVQIGLQCQDLQ 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157426875  562 SLSLANLGMMGKVVYMPALSDMLKHCKRLRDLRLEQPYFSANAQFFQALSQCPSLQRLCLVSRSGTLQPDAVLAFMARCL 641
Cdd:pfam19729 481 VLSLANLGMLGKVNYMPALCEMLKHCKQLKDLRLEQPYFSANAQFFQALSHCSSLQRLCIVSRSGTFQPDAVLSFMASCL 560

                         570       580       590
                  ....*....|....*....|....*....|....
gi 157426875  642 QVVMCHLFTGESLATCKSLQQSLLRSFQAERPAL 675
Cdd:pfam19729 561 HVVMCHMFTGETLVACKNLQQSLLRSFQAERPAL 594
F-box_FBXL18 cd22128
F-box domain found in F-box/LRR-repeat protein 18 (FBXL18) and similar proteins; FBXL18, also ...
 28-71 3.42e-19

F-box domain found in F-box/LRR-repeat protein 18 (FBXL18) and similar proteins; FBXL18, also called F-box and leucine-rich repeat protein 18, is a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It promotes glioma progression by promoting K63-linked ubiquitination of Akt. It targets leucine-rich repeat kinase 2 (LRRK2) for proteasomal degradation and attenuates cell toxicity. FBXL18 also regulates apoptosis by mediating ubiquitin-dependent proteasomal degradation of the pro-apoptotic protein FBXL7 that may impact cellular processes involved in cell cycle progression. 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: 438900  Cd Length: 44  Bit Score: 81.33  E-value: 3.42e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157426875  28 LLGFSDEILLHILSHVPSTDLILNVRRTCRKLAALCLDKSLIHT 71
Cdd:cd22128    1 LTEFSDEILLNILRFVPSTDLILNVRRTCRKLATLCLDKSLIHS 44
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 33-68 4.27e-05

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 41.31  E-value: 4.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 157426875   33 DEILLHILSHVPSTDLiLNVRRTCRKLAALCLDKSL 68
Cdd:pfam12937   6 DEILLQIFSYLDPKDL-LRLALVCRRWRELASDDSL 40
F-box_ScMFB1-like cd22146
F-box domain found in Saccharomyces cerevisiae mitochondrial F-box protein MFB1 (ScMFB1) and ...
 28-70 8.15e-05

F-box domain found in Saccharomyces cerevisiae mitochondrial F-box protein MFB1 (ScMFB1) and similar proteins; ScMFB1 is a novel mitochondria-associated F-box protein that functions to increase mitochondrial connectivity in yeast. ScMFB1 acts as a key component of a Skp1-Cdc53/Cullin-F-box protein (SCF) ubiquitin ligase complex machinery that regulates mitochondrial dynamics throughout the yeast's entire life cycle. It interacts with Skp1p in an F-box-dependent 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: 438917  Cd Length: 42  Bit Score: 40.32  E-value: 8.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 157426875  28 LLGFSDEILLHILSHVPSTDlILNVRRTCRKLAALCLDKSLIH 70
Cdd:cd22146    1 LLGLPLEILFEILIYLDIPD-ILNLSKTCRFLYVLLNDEILWR 42
F-box_FBXO6-like cd22168
F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily ...
 33-56 3.03e-04

F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily includes FBXO6 and FBXO44. FBXO6, also called FBX6, F-box protein that recognizes sugar chains 2 (FBS2), or F-box/G-domain protein 2 (FBG2), is a substrate-recognition component of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. It is involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins, by recognizing and binding sugar chains on unfolded glycoproteins that are retro-translocated into the cytosol and promoting their ubiquitination and subsequent degradation. FBXO6 can recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. It also recognizes sulfated glycans. FBXO6 is involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. FBXO44, also called FBXO6A, FBX44, or F-box/G-domain protein 3 (FBG3), is a substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It interacts with SKP1 and CUL1. FBXO44 mediates BRCA1 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: 438939 [Multi-domain]  Cd Length: 82  Bit Score: 39.96  E-value: 3.03e-04
                         10        20
                 ....*....|....*....|....
gi 157426875  33 DEILLHILSHVPSTDLILNVRRTC 56
Cdd:cd22168    9 EDVLLEILSLVPARDLILSCRLVC 32
FBOX smart00256
A Receptor for Ubiquitination Targets;
33-70 9.92e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 37.42  E-value: 9.92e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 157426875    33 DEILLHILSHVPSTDLiLNVRRTCRKLAALCLDKSLIH 70
Cdd:smart00256   3 DEILEEILSKLDPKDL-LRLRKVSRKWRSLIDSHDFWF 39
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 33-63 1.98e-03

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: 36.27  E-value: 1.98e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 157426875  33 DEILLHILSHVPSTDLiLNVRRTCRKLAALC 63
Cdd:cd09917    5 DEILLKILSYLDPRDL-LRLSLVCKRWRELA 34
F-box_FBXO24 cd22098
F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called ...
 27-63 6.22e-03

F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called FBX24, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It recognizes deacetylated nucleoside diphosphate kinase A (NDPK-A) to enhance its 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: 438870  Cd Length: 47  Bit Score: 35.38  E-value: 6.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157426875  27 HLLGFSDEILLHILSHVPSTDlILNVRRTCRKLAALC 63
Cdd:cd22098    1 SLLDLPPEILDRIISFLPVKD-IVSLGQTCRYFHEVC 36
 
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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