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Conserved domains on  [gi|23297438|gb|AAN12969|]
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putative F-box protein AtFBL18 [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 ...
 62-108 2.36e-23

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: 92.92  E-value: 2.36e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 23297438    62 PEMRSLTLKGKPHFADYNLVPDGWGGYAWPWIEAMAAKSSSLEEIRM 108
Cdd:pfam18791   1 PRLRSLTLKGKPRFADFNLVPEDWGGYATPWIEALARAYPWLEELRL 47
F-box_5 super family cl39836
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
 4-43 4.73e-15

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.


The actual alignment was detected with superfamily member pfam18511:

Pssm-ID: 436553  Cd Length: 42  Bit Score: 69.14  E-value: 4.73e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 23297438     4 RFPPKVLEHILSFIDSNEDRNSVSLVCKSWFETERKTRKR 43
Cdd:pfam18511   3 GFPDEVLECVLPYITSPRDRNAVSLVCKRWYRIEALTRKH 42
FBXL3_LRR-like super family cl45928
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 99-323 3.00e-08

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


The actual alignment was detected with superfamily member cd23951:

Pssm-ID: 480268 [Multi-domain]  Cd Length: 349  Bit Score: 55.85  E-value: 3.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438  99 KSSSLEEIRMKRMVVTDECLEKIAASFKD-FKVLVLTSCEGFSTDGIAAIAATCRNLRVLELRECIVEDlggDWLSYFpe 177
Cdd:cd23951  92 HSSSLSSLAIDDTPVDDPSLQTLASSSSDtLELLKMKSCPRVSPRGILAVADHCQHLRELSLNYHLLSD---DLLLAL-- 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 178 SSTSLVSLDFSCLD--SE---------VKISDLERLVSRSPNLKSLKLNPAVTLDGLVSLLRCAPQLTELGTGSFAAQlk 246
Cdd:cd23951 167 SSEEHVRLEHLRIDvvSEndgpmplhqISKESWDALIKHSPDVNLVMYFFVLEDEDFDPFFRSYTPVTHLYFGRSVPK-- 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 247 peafSKLSEAFSNCKQLQSL----SGLwDVLPEYLPALYSVCPGLTSLNLSYATVRMPDLVELLRRCS-KLQKLWVMD-- 319
Cdd:cd23951 245 ----AVLGRVGQHCPRLVELvvcaNGN-SPIDEELIRIAKNCKQLSSLGLGECEVSCSALVEFAKLCGpRLTELYVMEev 319


                ....
gi 23297438 320 LIED 323
Cdd:cd23951 320 LVED 323
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 280-488 2.19e-07

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


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 51.94  E-value: 2.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 280 LYSVCPGLTSLNLSYATVRMPDLvELLRRCSKLQKLWVM--DLIEDKGLEAVASYCKELRELrvfpsepDLDA-TNIplT 356
Cdd:cd09293  23 LRILHSGLEWLELYMCPISDPPL-DQLSNCNKLKKLILPgsKLIDDEGLIALAQSCPNLQVL-------DLRAcENI--T 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 357 EQGLVFVSKGCRKLESV----LYFCVQFTNAALFTIARKRPNLKC--FRLCVIEpfapdyktneplDKGFKAIAEGCRD- 429
Cdd:cd09293  93 DSGIVALATNCPKLQTInlgrHRNGHLITDVSLSALGKNCTFLQTvgFAGCDVT------------DKGVWELASGCSKs 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23297438 430 LRRLSVSG--LLSDKAFKYIgkhakkvrmlsiafagdsdLMLHhllsGCESLKKLEIRDCP 488
Cdd:cd09293 161 LERLSLNNcrNLTDQSIPAI-------------------LASN----YFPNLSVLEFRGCP 198
 
Name Accession Description Interval E-value
Transp_inhibit pfam18791
Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response ...
 62-108 2.36e-23

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: 92.92  E-value: 2.36e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 23297438    62 PEMRSLTLKGKPHFADYNLVPDGWGGYAWPWIEAMAAKSSSLEEIRM 108
Cdd:pfam18791   1 PRLRSLTLKGKPRFADFNLVPEDWGGYATPWIEALARAYPWLEELRL 47
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
 4-43 4.73e-15

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: 69.14  E-value: 4.73e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 23297438     4 RFPPKVLEHILSFIDSNEDRNSVSLVCKSWFETERKTRKR 43
Cdd:pfam18511   3 GFPDEVLECVLPYITSPRDRNAVSLVCKRWYRIEALTRKH 42
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 4-41 4.99e-12

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: 60.56  E-value: 4.99e-12
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 23297438   4 RFPPKVLEHILSFIDSNEDRNSVSLVCKSWFETERKTR 41
Cdd:cd22159   3 LLPDEILELIFSYLSDPWDRNSCSLVCKRWYRLERATR 40
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 99-323 3.00e-08

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 55.85  E-value: 3.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438  99 KSSSLEEIRMKRMVVTDECLEKIAASFKD-FKVLVLTSCEGFSTDGIAAIAATCRNLRVLELRECIVEDlggDWLSYFpe 177
Cdd:cd23951  92 HSSSLSSLAIDDTPVDDPSLQTLASSSSDtLELLKMKSCPRVSPRGILAVADHCQHLRELSLNYHLLSD---DLLLAL-- 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 178 SSTSLVSLDFSCLD--SE---------VKISDLERLVSRSPNLKSLKLNPAVTLDGLVSLLRCAPQLTELGTGSFAAQlk 246
Cdd:cd23951 167 SSEEHVRLEHLRIDvvSEndgpmplhqISKESWDALIKHSPDVNLVMYFFVLEDEDFDPFFRSYTPVTHLYFGRSVPK-- 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 247 peafSKLSEAFSNCKQLQSL----SGLwDVLPEYLPALYSVCPGLTSLNLSYATVRMPDLVELLRRCS-KLQKLWVMD-- 319
Cdd:cd23951 245 ----AVLGRVGQHCPRLVELvvcaNGN-SPIDEELIRIAKNCKQLSSLGLGECEVSCSALVEFAKLCGpRLTELYVMEev 319


                ....
gi 23297438 320 LIED 323
Cdd:cd23951 320 LVED 323
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 280-488 2.19e-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: 51.94  E-value: 2.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 280 LYSVCPGLTSLNLSYATVRMPDLvELLRRCSKLQKLWVM--DLIEDKGLEAVASYCKELRELrvfpsepDLDA-TNIplT 356
Cdd:cd09293  23 LRILHSGLEWLELYMCPISDPPL-DQLSNCNKLKKLILPgsKLIDDEGLIALAQSCPNLQVL-------DLRAcENI--T 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 357 EQGLVFVSKGCRKLESV----LYFCVQFTNAALFTIARKRPNLKC--FRLCVIEpfapdyktneplDKGFKAIAEGCRD- 429
Cdd:cd09293  93 DSGIVALATNCPKLQTInlgrHRNGHLITDVSLSALGKNCTFLQTvgFAGCDVT------------DKGVWELASGCSKs 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23297438 430 LRRLSVSG--LLSDKAFKYIgkhakkvrmlsiafagdsdLMLHhllsGCESLKKLEIRDCP 488
Cdd:cd09293 161 LERLSLNNcrNLTDQSIPAI-------------------LASN----YFPNLSVLEFRGCP 198
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
133-315 3.16e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 3.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 133 LTSCEGFSTDGIAAIAAtCRNLRVLELRECIVEDLGgDWLSYFpessTSLVSLDFScldsEVKISDLERLVSRSPNLKSL 212
Cdd:COG4886  95 LTNLTELDLSGNEELSN-LTNLESLDLSGNQLTDLP-EELANL----TNLKELDLS----NNQLTDLPEPLGNLTNLKSL 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 213 KL--NPAVTLDGLVSLLrcaPQLTELG-TGSfaaqlkpeAFSKLSEAFSNCKQLQSLS----GLWDvLPEYLPALysvcP 285
Cdd:COG4886 165 DLsnNQLTDLPEELGNL---TNLKELDlSNN--------QITDLPEPLGNLTNLEELDlsgnQLTD-LPEPLANL----T 228

                       170       180       190
                ....*....|....*....|....*....|.
gi 23297438 286 GLTSLNLSYATVR-MPDLVELlrrcSKLQKL 315
Cdd:COG4886 229 NLETLDLSNNQLTdLPELGNL----TNLEEL 255
FBOX smart00256
A Receptor for Ubiquitination Targets;
5-33 1.78e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.26  E-value: 1.78e-03
                           10        20
                   ....*....|....*....|....*....
gi 23297438      5 FPPKVLEHILSFIDSNeDRNSVSLVCKSW 33
Cdd:smart00256   1 LPDEILEEILSKLDPK-DLLRLRKVSRKW 28
 
Name Accession Description Interval E-value
Transp_inhibit pfam18791
Transport inhibitor response 1 protein domain; The F-box protein Transport inhibitor response ...
 62-108 2.36e-23

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: 92.92  E-value: 2.36e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 23297438    62 PEMRSLTLKGKPHFADYNLVPDGWGGYAWPWIEAMAAKSSSLEEIRM 108
Cdd:pfam18791   1 PRLRSLTLKGKPRFADFNLVPEDWGGYATPWIEALARAYPWLEELRL 47
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
 4-43 4.73e-15

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: 69.14  E-value: 4.73e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 23297438     4 RFPPKVLEHILSFIDSNEDRNSVSLVCKSWFETERKTRKR 43
Cdd:pfam18511   3 GFPDEVLECVLPYITSPRDRNAVSLVCKRWYRIEALTRKH 42
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 4-41 4.99e-12

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: 60.56  E-value: 4.99e-12
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 23297438   4 RFPPKVLEHILSFIDSNEDRNSVSLVCKSWFETERKTR 41
Cdd:cd22159   3 LLPDEILELIFSYLSDPWDRNSCSLVCKRWYRLERATR 40
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 99-323 3.00e-08

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 55.85  E-value: 3.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438  99 KSSSLEEIRMKRMVVTDECLEKIAASFKD-FKVLVLTSCEGFSTDGIAAIAATCRNLRVLELRECIVEDlggDWLSYFpe 177
Cdd:cd23951  92 HSSSLSSLAIDDTPVDDPSLQTLASSSSDtLELLKMKSCPRVSPRGILAVADHCQHLRELSLNYHLLSD---DLLLAL-- 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 178 SSTSLVSLDFSCLD--SE---------VKISDLERLVSRSPNLKSLKLNPAVTLDGLVSLLRCAPQLTELGTGSFAAQlk 246
Cdd:cd23951 167 SSEEHVRLEHLRIDvvSEndgpmplhqISKESWDALIKHSPDVNLVMYFFVLEDEDFDPFFRSYTPVTHLYFGRSVPK-- 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 247 peafSKLSEAFSNCKQLQSL----SGLwDVLPEYLPALYSVCPGLTSLNLSYATVRMPDLVELLRRCS-KLQKLWVMD-- 319
Cdd:cd23951 245 ----AVLGRVGQHCPRLVELvvcaNGN-SPIDEELIRIAKNCKQLSSLGLGECEVSCSALVEFAKLCGpRLTELYVMEev 319


                ....
gi 23297438 320 LIED 323
Cdd:cd23951 320 LVED 323
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 280-488 2.19e-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: 51.94  E-value: 2.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 280 LYSVCPGLTSLNLSYATVRMPDLvELLRRCSKLQKLWVM--DLIEDKGLEAVASYCKELRELrvfpsepDLDA-TNIplT 356
Cdd:cd09293  23 LRILHSGLEWLELYMCPISDPPL-DQLSNCNKLKKLILPgsKLIDDEGLIALAQSCPNLQVL-------DLRAcENI--T 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 357 EQGLVFVSKGCRKLESV----LYFCVQFTNAALFTIARKRPNLKC--FRLCVIEpfapdyktneplDKGFKAIAEGCRD- 429
Cdd:cd09293  93 DSGIVALATNCPKLQTInlgrHRNGHLITDVSLSALGKNCTFLQTvgFAGCDVT------------DKGVWELASGCSKs 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23297438 430 LRRLSVSG--LLSDKAFKYIgkhakkvrmlsiafagdsdLMLHhllsGCESLKKLEIRDCP 488
Cdd:cd09293 161 LERLSLNNcrNLTDQSIPAI-------------------LASN----YFPNLSVLEFRGCP 198
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
133-315 3.16e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 3.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 133 LTSCEGFSTDGIAAIAAtCRNLRVLELRECIVEDLGgDWLSYFpessTSLVSLDFScldsEVKISDLERLVSRSPNLKSL 212
Cdd:COG4886  95 LTNLTELDLSGNEELSN-LTNLESLDLSGNQLTDLP-EELANL----TNLKELDLS----NNQLTDLPEPLGNLTNLKSL 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 213 KL--NPAVTLDGLVSLLrcaPQLTELG-TGSfaaqlkpeAFSKLSEAFSNCKQLQSLS----GLWDvLPEYLPALysvcP 285
Cdd:COG4886 165 DLsnNQLTDLPEELGNL---TNLKELDlSNN--------QITDLPEPLGNLTNLEELDlsgnQLTD-LPEPLANL----T 228

                       170       180       190
                ....*....|....*....|....*....|.
gi 23297438 286 GLTSLNLSYATVR-MPDLVELlrrcSKLQKL 315
Cdd:COG4886 229 NLETLDLSNNQLTdLPELGNL----TNLEEL 255
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 112-267 5.18e-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: 47.71  E-value: 5.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 112 VVTDECLEKIAASFKDFKVLVLTSCEGFSTDGIAAIAATCRNLRVLEL---RECI-VEDLGgdwLSYFPESSTSLVSLDF 187
Cdd:cd09293  64 LIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHlITDVS---LSALGKNCTFLQTVGF 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 188 SCLDsevkISD--LERLVS-RSPNLKSLKLNpavtldglvsllRCaPQLTElgtGSFAAQLKPEAFSKLSE-AFSNCKQL 263
Cdd:cd09293 141 AGCD----VTDkgVWELASgCSKSLERLSLN------------NC-RNLTD---QSIPAILASNYFPNLSVlEFRGCPLI 200


                ....
gi 23297438 264 QSLS 267
Cdd:cd09293 201 TDFS 204
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
 4-36 2.90e-04

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: 38.42  E-value: 2.90e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 23297438   4 RFPPKVLEHILSFIDSNEDRNsVSLVCKSWFET 36
Cdd:cd22111   3 RLPSRVLEVIFSYLDLPDLRN-CSLVCKSWYRL 34
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 4-35 3.12e-04

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: 38.50  E-value: 3.12e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 23297438   4 RFPPKVLEHILSFIdSNEDRNSVSLVCKSWFE 35
Cdd:cd22121   2 ALPEEILVHIFRHL-SLRDRYAAAQVCKHWRE 32
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 4-35 6.52e-04

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: 37.62  E-value: 6.52e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 23297438   4 RFPPKVLEHILSFIdSNEDRNSVSLVCKSWFE 35
Cdd:cd22104   3 NLPSVVLVHIFSYL-PPRDRLRASSTCRRWRE 33
FBXL21_LRR cd23956
Leucine-rich repeat domain of F-box/LRR-repeat protein 21; FBXL21 (F-box/LRR-repeat protein 21) ...
 100-166 1.54e-03

Leucine-rich repeat domain of F-box/LRR-repeat protein 21; FBXL21 (F-box/LRR-repeat protein 21) stabilizes CRY repressor proteins through ubiquitination and therefore counteracts FBXL3. FBXL3 (F-box/LRR-repeat protein 3), together with SKP1 (S-phase-kinase-associated protein-1) and the cullin subunit CUL1, forms a Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complex that ubiquitinates CRYs mediating their degradation. This plays an important role in oscillation of the circadian clock. FBXL21 has also been shown to regulate myoblast differentiation and sarcomere architecture via Myozenin 1 (MYOZ1; calsarcin-2) ubiquitination and NFAT signaling.


Pssm-ID: 467831 [Multi-domain]  Cd Length: 350  Bit Score: 41.01  E-value: 1.54e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23297438 100 SSSLEEIRMKRMVVTDECLEKIAASFKD-FKVLVLTSCEGFSTDGIAAIAATCRNLRVLELRECIVED 166
Cdd:cd23956  93 SKSLSSIKIEDTPVDDPSLKILVANNSDtLRLLKMSSCPHVSSDGILCVADHCQGLRELALNYYILSD 160
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 151-313 1.58e-03

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: 40.39  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 151 CRNLRVLELRECIVEDLGGDWLSYfpesSTSLVSLdfsCLDSEVKISD--LERLVSRSPNLK--SLKLNPAVTLDGLVSL 226
Cdd:cd09293  27 HSGLEWLELYMCPISDPPLDQLSN----CNKLKKL---ILPGSKLIDDegLIALAQSCPNLQvlDLRACENITDSGIVAL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 227 LRCAPQLT--ELGTGSFAAQLKPEAFSKLSEafsNCKQLQSL---------SGLWDVLPEYLPALYSV----CPGLT--S 289
Cdd:cd09293 100 ATNCPKLQtiNLGRHRNGHLITDVSLSALGK---NCTFLQTVgfagcdvtdKGVWELASGCSKSLERLslnnCRNLTdqS 176

                       170       180
                ....*....|....*....|....*
gi 23297438 290 LNLSYATVRMPDL-VELLRRCSKLQ 313
Cdd:cd09293 177 IPAILASNYFPNLsVLEFRGCPLIT 201
FBOX smart00256
A Receptor for Ubiquitination Targets;
5-33 1.78e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.26  E-value: 1.78e-03
                           10        20
                   ....*....|....*....|....*....
gi 23297438      5 FPPKVLEHILSFIDSNeDRNSVSLVCKSW 33
Cdd:smart00256   1 LPDEILEEILSKLDPK-DLLRLRKVSRKW 28
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 100-237 1.81e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 40.80  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 100 SSSLEEIRMKRMVVTDECLEKIAASFK---DFKVLVLtSCEGFSTDGIAAIA---ATCRNLRVLELRECIVEDLGGDWLS 173
Cdd:cd00116 136 PPALEKLVLGRNRLEGASCEALAKALRanrDLKELNL-ANNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALA 214

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23297438 174 YFPESSTSLVSLDFS-CLDSEVKISDL-ERLVSRSPNLKSLKL-NPAVTLDGLVSLLR-CA--PQLTELG 237
Cdd:cd00116 215 ETLASLKSLEVLNLGdNNLTDAGAAALaSALLSPNISLLTLSLsCNDITDDGAKDLAEvLAekESLLELD 284
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 5-33 2.09e-03

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: 36.16  E-value: 2.09e-03
                        10        20
                ....*....|....*....|....*....
gi 23297438   5 FPPKVLEHILSFIDSNEDRNSVSLVCKSW 33
Cdd:cd22110   4 LPEEILEYILSYLSPYGDLKSAALVCKRW 32
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 3-33 4.97e-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: 34.73  E-value: 4.97e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 23297438   3 LRFPPKVLEHILSFIDSnEDRNSVSLVCKSW 33
Cdd:cd09917   1 SDLPDEILLKILSYLDP-RDLLRLSLVCKRW 30
 
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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