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Conserved domains on  [gi|18412567|ref|NP_567135|]
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F-box/RNI-like superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Transp_inhibit pfam18791
Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response ...
66-112 1.78e-28

Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response 1 (TIR1) is a receptor for auxin, triggering an auxin-enhanced and ubiquitin-mediated degradation of substrates. The targets are recruited via interaction with the leucine-rich repeat region of the protein. This Pfam entry represents a specific unit of the LRR region, including an insertion of one short alpha-helix in the loop between the beta-strand and the following helix. It shares some sequence homology with a unit with similar structure of Coronatine-insensitive protein 1.


:

Pssm-ID: 465867  Cd Length: 47  Bit Score: 107.17  E-value: 1.78e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18412567    66 PKVRSVELKGKPHFADFNLVPDGWGGYVYPWIEAMSSSYTWLEEIRL 112
Cdd:pfam18791   1 PRLRSLTLKGKPRFADFNLVPEDWGGYATPWIEALARAYPWLEELRL 47
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
8-47 4.82e-18

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: 77.61  E-value: 4.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18412567     8 SFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCRRK 47
Cdd:pfam18511   3 GFPDEVLECVLPYITSPRDRNAVSLVCKRWYRIEALTRKH 42
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
127-319 4.24e-07

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


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 127 KSFKNFKVLVLSSCEGFSTdglaaiaatCRNLKELDLRESDVDDVsGHWLSHFpdtyTSLVSLNISclasEVSFSALERL 206
Cdd:COG4886  93 GDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTDL-PEELANL----TNLKELDLS----NNQLTDLPEP 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 207 VTRCPNLKSLKLNRAvPLEKLATLLQRAPQLEELgtggytaevrpDVY----SGLSVALSGCKELRCLS----GFWDavp 278
Cdd:COG4886 155 LGNLTNLKSLDLSNN-QLTDLPEELGNLTNLKEL-----------DLSnnqiTDLPEPLGNLTNLEELDlsgnQLTD--- 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18412567 279 ayLPAVYSVCSRLTTLNLSYATVQSydlVKLLCQCPKLQRL 319
Cdd:COG4886 220 --LPEPLANLTNLETLDLSNNQLTD---LPELGNLTNLEEL 255
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
286-400 4.62e-04

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: 41.93  E-value: 4.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 286 SVCSRLTTLNLSYATVQSYDLVKLLCqCPKLQRLwVLD---YIEDAGLEVLASTCKDLRELRVFPSEpfvmepnvALTEQ 362
Cdd:cd09293  25 ILHSGLEWLELYMCPISDPPLDQLSN-CNKLKKL-ILPgskLIDDEGLIALAQSCPNLQVLDLRACE--------NITDS 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18412567 363 GLVSVSMGCPKLESV----LYFCRQMTNAALITIARNRPNMT 400
Cdd:cd09293  95 GIVALATNCPKLQTInlgrHRNGHLITDVSLSALGKNCTFLQ 136
 
Name Accession Description Interval E-value
Transp_inhibit pfam18791
Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response ...
66-112 1.78e-28

Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response 1 (TIR1) is a receptor for auxin, triggering an auxin-enhanced and ubiquitin-mediated degradation of substrates. The targets are recruited via interaction with the leucine-rich repeat region of the protein. This Pfam entry represents a specific unit of the LRR region, including an insertion of one short alpha-helix in the loop between the beta-strand and the following helix. It shares some sequence homology with a unit with similar structure of Coronatine-insensitive protein 1.


Pssm-ID: 465867  Cd Length: 47  Bit Score: 107.17  E-value: 1.78e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18412567    66 PKVRSVELKGKPHFADFNLVPDGWGGYVYPWIEAMSSSYTWLEEIRL 112
Cdd:pfam18791   1 PRLRSLTLKGKPRFADFNLVPEDWGGYATPWIEALARAYPWLEELRL 47
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
8-47 4.82e-18

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: 77.61  E-value: 4.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18412567     8 SFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCRRK 47
Cdd:pfam18511   3 GFPDEVLECVLPYITSPRDRNAVSLVCKRWYRIEALTRKH 42
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
8-45 3.01e-13

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: 64.02  E-value: 3.01e-13
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 18412567   8 SFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCR 45
Cdd:cd22159   3 LLPDEILELIFSYLSDPWDRNSCSLVCKRWYRLERATR 40
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
127-319 4.24e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 127 KSFKNFKVLVLSSCEGFSTdglaaiaatCRNLKELDLRESDVDDVsGHWLSHFpdtyTSLVSLNISclasEVSFSALERL 206
Cdd:COG4886  93 GDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTDL-PEELANL----TNLKELDLS----NNQLTDLPEP 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 207 VTRCPNLKSLKLNRAvPLEKLATLLQRAPQLEELgtggytaevrpDVY----SGLSVALSGCKELRCLS----GFWDavp 278
Cdd:COG4886 155 LGNLTNLKSLDLSNN-QLTDLPEELGNLTNLKEL-----------DLSnnqiTDLPEPLGNLTNLEELDlsgnQLTD--- 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18412567 279 ayLPAVYSVCSRLTTLNLSYATVQSydlVKLLCQCPKLQRL 319
Cdd:COG4886 220 --LPEPLANLTNLETLDLSNNQLTD---LPELGNLTNLEEL 255
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
116-224 4.65e-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: 51.17  E-value: 4.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 116 VVTDDCLELIAKSFKNFKVLVLSSCEGFSTDGLAAIAATCRNLKELDLRESDvddvSGHWLshfpdTYTSLVSL--NISC 193
Cdd:cd09293  64 LIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHR----NGHLI-----TDVSLSALgkNCTF 134
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18412567 194 LAS------EVSFSALERLVTRC-PNLKSLKLNRAVPL 224
Cdd:cd09293 135 LQTvgfagcDVTDKGVWELASGCsKSLERLSLNNCRNL 172
FBOX smart00256
A Receptor for Ubiquitination Targets;
9-45 1.30e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 39.34  E-value: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 18412567      9 FPEEVLEHVFSFIQLdKDRNSVSLVCKSWYEIERWCR 45
Cdd:smart00256   1 LPDEILEEILSKLDP-KDLLRLRKVSRKWRSLIDSHD 36
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
286-400 4.62e-04

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: 41.93  E-value: 4.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 286 SVCSRLTTLNLSYATVQSYDLVKLLCqCPKLQRLwVLD---YIEDAGLEVLASTCKDLRELRVFPSEpfvmepnvALTEQ 362
Cdd:cd09293  25 ILHSGLEWLELYMCPISDPPLDQLSN-CNKLKKL-ILPgskLIDDEGLIALAQSCPNLQVLDLRACE--------NITDS 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18412567 363 GLVSVSMGCPKLESV----LYFCRQMTNAALITIARNRPNMT 400
Cdd:cd09293  95 GIVALATNCPKLQTInlgrHRNGHLITDVSLSALGKNCTFLQ 136
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
184-344 1.16e-03

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: 41.65  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567   184 TSLVSLNIS----CLASEVSF---------SALERLVTRCPNLKSLKLNRA-----VPLEK-LATLLQRAPQLEEL---- 240
Cdd:pfam19729 260 RSLVSLNLSgcvhCLLPDSLLrkaeddidsSIVETLVACCPNLRHLNLSAAhhhssEGLGGhLCALLARLKHLRSLslpv 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567   241 -----------------------GTGGYTAEVR---------------PDVYSGLSVALSGCKELRCL----SGFWDAVP 278
Cdd:pfam19729 340 cavadsaktadkspsqtdlassaVPLGFGKKVRigvqtyprdsseqasPDPTSVFWTLLKGCPFLEELeligSNFSSAMP 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567   279 AYLPAV---YSVCSR--------------LTTL-NLSYATVQSY----DLVKLLCQCPKLQRLWV--------LDYIedA 328
Cdd:pfam19729 420 RNEPAIrnsLPPCARaqsvgdsevaaigqLAFLrRLTLAQLPGIltgsGLVQIGLQCQDLQVLSLanlgmlgkVNYM--P 497
                         250
                  ....*....|....*.
gi 18412567   329 GLEVLASTCKDLRELR 344
Cdd:pfam19729 498 ALCEMLKHCKQLKDLR 513
 
Name Accession Description Interval E-value
Transp_inhibit pfam18791
Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response ...
66-112 1.78e-28

Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response 1 (TIR1) is a receptor for auxin, triggering an auxin-enhanced and ubiquitin-mediated degradation of substrates. The targets are recruited via interaction with the leucine-rich repeat region of the protein. This Pfam entry represents a specific unit of the LRR region, including an insertion of one short alpha-helix in the loop between the beta-strand and the following helix. It shares some sequence homology with a unit with similar structure of Coronatine-insensitive protein 1.


Pssm-ID: 465867  Cd Length: 47  Bit Score: 107.17  E-value: 1.78e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18412567    66 PKVRSVELKGKPHFADFNLVPDGWGGYVYPWIEAMSSSYTWLEEIRL 112
Cdd:pfam18791   1 PRLRSLTLKGKPRFADFNLVPEDWGGYATPWIEALARAYPWLEELRL 47
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
8-47 4.82e-18

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: 77.61  E-value: 4.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18412567     8 SFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCRRK 47
Cdd:pfam18511   3 GFPDEVLECVLPYITSPRDRNAVSLVCKRWYRIEALTRKH 42
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
8-45 3.01e-13

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: 64.02  E-value: 3.01e-13
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 18412567   8 SFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCR 45
Cdd:cd22159   3 LLPDEILELIFSYLSDPWDRNSCSLVCKRWYRLERATR 40
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
127-319 4.24e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 127 KSFKNFKVLVLSSCEGFSTdglaaiaatCRNLKELDLRESDVDDVsGHWLSHFpdtyTSLVSLNISclasEVSFSALERL 206
Cdd:COG4886  93 GDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTDL-PEELANL----TNLKELDLS----NNQLTDLPEP 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 207 VTRCPNLKSLKLNRAvPLEKLATLLQRAPQLEELgtggytaevrpDVY----SGLSVALSGCKELRCLS----GFWDavp 278
Cdd:COG4886 155 LGNLTNLKSLDLSNN-QLTDLPEELGNLTNLKEL-----------DLSnnqiTDLPEPLGNLTNLEELDlsgnQLTD--- 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18412567 279 ayLPAVYSVCSRLTTLNLSYATVQSydlVKLLCQCPKLQRL 319
Cdd:COG4886 220 --LPEPLANLTNLETLDLSNNQLTD---LPELGNLTNLEEL 255
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
116-224 4.65e-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: 51.17  E-value: 4.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 116 VVTDDCLELIAKSFKNFKVLVLSSCEGFSTDGLAAIAATCRNLKELDLRESDvddvSGHWLshfpdTYTSLVSL--NISC 193
Cdd:cd09293  64 LIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHR----NGHLI-----TDVSLSALgkNCTF 134
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18412567 194 LAS------EVSFSALERLVTRC-PNLKSLKLNRAVPL 224
Cdd:cd09293 135 LQTvgfagcDVTDKGVWELASGCsKSLERLSLNNCRNL 172
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
8-40 2.12e-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: 44.63  E-value: 2.12e-06
                        10        20        30
                ....*....|....*....|....*....|...
gi 18412567   8 SFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEI 40
Cdd:cd22110   3 DLPEEILEYILSYLSPYGDLKSAALVCKRWHRI 35
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
10-40 3.33e-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: 43.89  E-value: 3.33e-06
                        10        20        30
                ....*....|....*....|....*....|.
gi 18412567  10 PEEVLEHVFSFIQLDkDRNSVSLVCKSWYEI 40
Cdd:cd22121   4 PEEILVHIFRHLSLR-DRYAAAQVCKHWREA 33
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
7-40 2.15e-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: 41.66  E-value: 2.15e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 18412567   7 LSFPEEVLEHVFSFiqLD-KDRNSVSLVCKSWYEI 40
Cdd:cd09917   1 SDLPDEILLKILSY--LDpRDLLRLSLVCKRWREL 33
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
9-38 4.87e-05

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: 40.73  E-value: 4.87e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 18412567   9 FPEEVLEHVFSFIQLdKDRNSVSLVCKSWY 38
Cdd:cd22111   4 LPSRVLEVIFSYLDL-PDLRNCSLVCKSWY 32
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
10-39 7.67e-05

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: 40.32  E-value: 7.67e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 18412567  10 PEEVLEHVFSFIQLdKDRNSVSLVCKSWYE 39
Cdd:cd22104   5 PSVVLVHIFSYLPP-RDRLRASSTCRRWRE 33
FBOX smart00256
A Receptor for Ubiquitination Targets;
9-45 1.30e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 39.34  E-value: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 18412567      9 FPEEVLEHVFSFIQLdKDRNSVSLVCKSWYEIERWCR 45
Cdd:smart00256   1 LPDEILEEILSKLDP-KDLLRLRKVSRKWRSLIDSHD 36
F-box-like pfam12937
F-box-like; This is an F-box-like family.
10-40 1.34e-04

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 39.77  E-value: 1.34e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 18412567    10 PEEVLEHVFSFiqLD-KDRNSVSLVCKSWYEI 40
Cdd:pfam12937   5 PDEILLQIFSY--LDpKDLLRLALVCRRWREL 34
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
9-40 1.37e-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: 1.37e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 18412567   9 FPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEI 40
Cdd:cd22095   5 LPEELLRNIFAFLPAEDLYQNISLVCRHWRDI 36
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
7-49 3.17e-04

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: 38.67  E-value: 3.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 18412567     7 LSFPEEVLEHVFSFIQLdKDRNSVSLVCKSWYEIERWCRRKVF 49
Cdd:pfam00646   2 LDLPDDLLLEILSRLDP-KDLLRLSLVSKRWRSLVDSLKLWKK 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
286-400 4.62e-04

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: 41.93  E-value: 4.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567 286 SVCSRLTTLNLSYATVQSYDLVKLLCqCPKLQRLwVLD---YIEDAGLEVLASTCKDLRELRVFPSEpfvmepnvALTEQ 362
Cdd:cd09293  25 ILHSGLEWLELYMCPISDPPLDQLSN-CNKLKKL-ILPgskLIDDEGLIALAQSCPNLQVLDLRACE--------NITDS 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18412567 363 GLVSVSMGCPKLESV----LYFCRQMTNAALITIARNRPNMT 400
Cdd:cd09293  95 GIVALATNCPKLQTInlgrHRNGHLITDVSLSALGKNCTFLQ 136
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
184-344 1.16e-03

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: 41.65  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567   184 TSLVSLNIS----CLASEVSF---------SALERLVTRCPNLKSLKLNRA-----VPLEK-LATLLQRAPQLEEL---- 240
Cdd:pfam19729 260 RSLVSLNLSgcvhCLLPDSLLrkaeddidsSIVETLVACCPNLRHLNLSAAhhhssEGLGGhLCALLARLKHLRSLslpv 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567   241 -----------------------GTGGYTAEVR---------------PDVYSGLSVALSGCKELRCL----SGFWDAVP 278
Cdd:pfam19729 340 cavadsaktadkspsqtdlassaVPLGFGKKVRigvqtyprdsseqasPDPTSVFWTLLKGCPFLEELeligSNFSSAMP 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412567   279 AYLPAV---YSVCSR--------------LTTL-NLSYATVQSY----DLVKLLCQCPKLQRLWV--------LDYIedA 328
Cdd:pfam19729 420 RNEPAIrnsLPPCARaqsvgdsevaaigqLAFLrRLTLAQLPGIltgsGLVQIGLQCQDLQVLSLanlgmlgkVNYM--P 497
                         250
                  ....*....|....*.
gi 18412567   329 GLEVLASTCKDLRELR 344
Cdd:pfam19729 498 ALCEMLKHCKQLKDLR 513
F-box_FBXO39 cd22108
F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called ...
8-40 4.10e-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: 35.47  E-value: 4.10e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 18412567   8 SFPEEVLEHVFSFIQlDKDRNSVSLVCKSWYEI 40
Cdd:cd22108   3 NLPDVCLRHVFRWLG-DRDRSRAALVCKRWNQA 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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