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Conserved domains on  [gi|2241021047|ref|XP_015571905|]
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F-box protein SKIP2-like [Ricinus communis]

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 ...
 297-428 1.97e-10

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 60.80  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241021047 297 DAGLIAISSTCPQLQVLQLSRTTDCTDDGLSAIATSCrsslRKLHVDAWSRF-GGRTIGDDGVLTVAAQCLRLQELVLMG 375
Cdd:cd09293    67 DEGLIALAQSCPNLQVLDLRACENITDSGIVALATNC----PKLQTINLGRHrNGHLITDVSLSALGKNCTFLQTVGFAG 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2241021047 376 VPISGSSLTVLASNC-RTLERLALCNTESVGDSEMGIIAAK--FNALKKLCIKNCP 428
Cdd:cd09293   143 CDVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCP 198
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 53-89 2.14e-10

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: 55.55  E-value: 2.14e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2241021047  53 SLPDECLATIFCKLS-CHDRNSCSLVCKRWKLIDSNSR 89
Cdd:cd22159     3 LLPDEILELIFSYLSdPWDRNSCSLVCKRWYRLERATR 40
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 297-428 1.97e-10

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 60.80  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241021047 297 DAGLIAISSTCPQLQVLQLSRTTDCTDDGLSAIATSCrsslRKLHVDAWSRF-GGRTIGDDGVLTVAAQCLRLQELVLMG 375
Cdd:cd09293    67 DEGLIALAQSCPNLQVLDLRACENITDSGIVALATNC----PKLQTINLGRHrNGHLITDVSLSALGKNCTFLQTVGFAG 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2241021047 376 VPISGSSLTVLASNC-RTLERLALCNTESVGDSEMGIIAAK--FNALKKLCIKNCP 428
Cdd:cd09293   143 CDVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCP 198
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 53-89 2.14e-10

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: 55.55  E-value: 2.14e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2241021047  53 SLPDECLATIFCKLS-CHDRNSCSLVCKRWKLIDSNSR 89
Cdd:cd22159     3 LLPDEILELIFSYLSdPWDRNSCSLVCKRWYRLERATR 40
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 52-92 1.34e-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: 42.14  E-value: 1.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2241021047  52 LSLPDECLATIFCKLSCHDRNSCSLVCKRWK-LIDSNSRHRL 92
Cdd:pfam00646   2 LDLPDDLLLEILSRLDPKDLLRLSLVSKRWRsLVDSLKLWKK 43
FBOX smart00256
A Receptor for Ubiquitination Targets;
54-88 5.40e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 40.50  E-value: 5.40e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2241021047   54 LPDECLATIFCKLSCHDRNSCSLVCKRWK-LIDSNS 88
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRsLIDSHD 36
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 297-428 1.97e-10

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 60.80  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241021047 297 DAGLIAISSTCPQLQVLQLSRTTDCTDDGLSAIATSCrsslRKLHVDAWSRF-GGRTIGDDGVLTVAAQCLRLQELVLMG 375
Cdd:cd09293    67 DEGLIALAQSCPNLQVLDLRACENITDSGIVALATNC----PKLQTINLGRHrNGHLITDVSLSALGKNCTFLQTVGFAG 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2241021047 376 VPISGSSLTVLASNC-RTLERLALCNTESVGDSEMGIIAAK--FNALKKLCIKNCP 428
Cdd:cd09293   143 CDVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCP 198
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 53-89 2.14e-10

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: 55.55  E-value: 2.14e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2241021047  53 SLPDECLATIFCKLS-CHDRNSCSLVCKRWKLIDSNSR 89
Cdd:cd22159     3 LLPDEILELIFSYLSdPWDRNSCSLVCKRWYRLERATR 40
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 305-452 1.55e-06

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: 49.25  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241021047 305 STCPQLQVLQLSRTTDCTDDGLSAIATSCrSSLRKLHVDAWSRfggrtIGDDGVLTVAAQCLRLQELVL----MGVPISG 380
Cdd:cd09293    49 SNCNKLKKLILPGSKLIDDEGLIALAQSC-PNLQVLDLRACEN-----ITDSGIVALATNCPKLQTINLgrhrNGHLITD 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2241021047 381 SSLTVLASNCRTLERLALCNTESVGDSEMGIIAAKFNALKKLCIKNCP-ISQSGIEAI--GGGCPNLVKLKVKRC 452
Cdd:cd09293   123 VSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGCSKSLERLSLNNCRnLTDQSIPAIlaSNYFPNLSVLEFRGC 197
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 53-81 1.95e-06

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: 44.27  E-value: 1.95e-06
                          10        20
                  ....*....|....*....|....*....
gi 2241021047  53 SLPDECLATIFCKLSCHDRNSCSLVCKRW 81
Cdd:cd22121     2 ALPEEILVHIFRHLSLRDRYAAAQVCKHW 30
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 332-460 9.26e-06

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: 46.94  E-value: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241021047 332 SCRSSLRKLHVDawsrfGGRTIGDDGVLTVAAQCLRLQELVLMGVP-ISGSSLTVLASNCRTLERLALCNTES---VGDS 407
Cdd:cd09293    49 SNCNKLKKLILP-----GSKLIDDEGLIALAQSCPNLQVLDLRACEnITDSGIVALATNCPKLQTINLGRHRNghlITDV 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2241021047 408 EMGIIAAKFNALKKLCIKNCPISQSGIEAIGGGC-PNLVKLKVKRCRGISEASV 460
Cdd:cd09293   124 SLSALGKNCTFLQTVGFAGCDVTDKGVWELASGCsKSLERLSLNNCRNLTDQSI 177
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 52-92 1.34e-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: 42.14  E-value: 1.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2241021047  52 LSLPDECLATIFCKLSCHDRNSCSLVCKRWK-LIDSNSRHRL 92
Cdd:pfam00646   2 LDLPDDLLLEILSRLDPKDLLRLSLVSKRWRsLVDSLKLWKK 43
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 52-84 1.85e-05

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 42.08  E-value: 1.85e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2241021047  52 LSLPDECLATIFCKLSCHDRNSCSLVCKRWKLI 84
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWREL 34
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 52-84 2.45e-05

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: 41.28  E-value: 2.45e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2241021047  52 LSLPDECLATIFCKLSCHDRNSCSLVCKRWKLI 84
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWREL 33
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 367-463 4.97e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 44.63  E-value: 4.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241021047 367 RLQELVLMGVPISGSSLTVLaSNCRTLERLALCNTESVGDSEMGIIAAKFNALKKLCIKNCP-ISQSGIEAIGGGCPNLV 445
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEnITDSGIVALATNCPKLQ 107

                          90       100
                  ....*....|....*....|.
gi 2241021047 446 KLKVKR---CRGISEASVRKL 463
Cdd:cd09293   108 TINLGRhrnGHLITDVSLSAL 128
FBOX smart00256
A Receptor for Ubiquitination Targets;
54-88 5.40e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 40.50  E-value: 5.40e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2241021047   54 LPDECLATIFCKLSCHDRNSCSLVCKRWK-LIDSNS 88
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRsLIDSHD 36
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 53-84 4.02e-04

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: 38.09  E-value: 4.02e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2241021047  53 SLPDECLATIFCKLSCH-DRNSCSLVCKRWKLI 84
Cdd:cd22110     3 DLPEEILEYILSYLSPYgDLKSAALVCKRWHRI 35
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
 53-89 5.94e-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: 37.55  E-value: 5.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2241021047  53 SLPDECLATIFCKLSCH-DRNSCSLVCKRWKLIDSNSR 89
Cdd:pfam18511   3 GFPDEVLECVLPYITSPrDRNAVSLVCKRWYRIEALTR 40
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 53-81 1.71e-03

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: 36.46  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 2241021047  53 SLPDECLATIFCKLSCHDRNSCSLVCKRW 81
Cdd:cd22104     3 NLPSVVLVHIFSYLPPRDRLRASSTCRRW 31
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 54-84 1.75e-03

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: 36.48  E-value: 1.75e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2241021047  54 LPDECLATIFCKLSCHD--RNsCSLVCKRWKLI 84
Cdd:cd22095     5 LPEELLRNIFAFLPAEDlyQN-ISLVCRHWRDI 36
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
 53-88 4.01e-03

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: 35.08  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2241021047  53 SLPDECLATIFCKLSCHDRNSCSLVCKRWKLIDSNS 88
Cdd:cd22114     3 SLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDE 38
F-box_FBXO39 cd22108
F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called ...
 53-84 7.27e-03

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: 34.70  E-value: 7.27e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2241021047  53 SLPDECLATIFCKLSCHDRNSCSLVCKRWKLI 84
Cdd:cd22108     3 NLPDVCLRHVFRWLGDRDRSRAALVCKRWNQA 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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