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Conserved domains on  [gi|190194416|ref|NP_077302|]
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F-box/LRR-repeat protein 15 [Homo sapiens]

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 ...
 139-266 3.73e-16

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: 75.83  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 139 CPRLQRLSLAHCDWVDGLALRGLADRCPALEELDLTACRQLKDEAIVYLAqRRGAGLRSLSLAVNAN---VGDAAVQELA 215
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALA-TNCPKLQTINLGRHRNghlITDVSLSALG 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 190194416 216 RNCPELHHLDLTGClRVGSDGVRTLAEYC-PVLRSLRVRHCHHVAESSLSRL 266
Cdd:cd09293  130 KNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAI 180
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 19-60 3.62e-13

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 62.52  E-value: 3.62e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 190194416  19 FLDLPWEDVLLPHVLNRVPLRQLLRLQRVSRAFRSLVQLHLA 60
Cdd:cd22126    1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFS 42
FBXL3_LRR-like super family cl45928
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 71-146 5.53e-04

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: 41.21  E-value: 5.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190194416  71 GPQIPRAALARLLRDAEGLQELALAPCHEWLSDEDLVPVLARNPQLRSVALGGCgQLSRRALGALAEGC-PRLQRLS 146
Cdd:cd23951  239 GRSVPKAVLGRVGQHCPRLVELVVCANGNSPIDEELIRIAKNCKQLSSLGLGEC-EVSCSALVEFAKLCgPRLTELY 314
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 139-266 3.73e-16

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: 75.83  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 139 CPRLQRLSLAHCDWVDGLALRGLADRCPALEELDLTACRQLKDEAIVYLAqRRGAGLRSLSLAVNAN---VGDAAVQELA 215
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALA-TNCPKLQTINLGRHRNghlITDVSLSALG 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 190194416 216 RNCPELHHLDLTGClRVGSDGVRTLAEYC-PVLRSLRVRHCHHVAESSLSRL 266
Cdd:cd09293  130 KNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAI 180
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 19-60 3.62e-13

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 62.52  E-value: 3.62e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 190194416  19 FLDLPWEDVLLPHVLNRVPLRQLLRLQRVSRAFRSLVQLHLA 60
Cdd:cd22126    1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFS 42
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 28-253 4.61e-05

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.40  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416  28 LLPHVLNRVPLRQLLRLQRVSRAFRSLvqLHLAGLRRFDAAQV-----GPQIPRAALARLLRDAEGLQELALAPCHE--- 99
Cdd:COG5238  133 LYLALPRRINLIQVLKDPLGGNAVHLL--GLAARLGLLAAISMakalqNNSVETVYLGCNQIGDEGIEELAEALTQNttv 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 100 ---WLSD--------EDLVPVLARNPQLRSVALGGcGQLSRRALGALAEGCP---RLQRLSLAHcDWVDGLALRGLAD-- 163
Cdd:COG5238  211 ttlWLKRnpigdegaEILAEALKGNKSLTTLDLSN-NQIGDEGVIALAEALKnntTVETLYLSG-NQIGAEGAIALAKal 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 164 -RCPALEELDLTAcRQLKDEAIVYLAQ--RRGAGLRSLSLAVNaNVGDAAVQELARNC---PELHHLDLTGClRVGSDGV 237
Cdd:COG5238  289 qGNTTLTSLDLSV-NRIGDEGAIALAEglQGNKTLHTLNLAYN-GIGAQGAIALAKALqenTTLHSLDLSDN-QIGDEGA 365

                        250
                 ....*....|....*....
gi 190194416 238 RTLAEY---CPVLRSLRVR 253
Cdd:COG5238  366 IALAKYlegNTTLRELNLG 384
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 19-55 1.90e-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: 38.29  E-value: 1.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 190194416   19 FLDLPweDVLLPHVLNRVPLRQLLRLQRVSRAFRSLV 55
Cdd:pfam00646   1 LLDLP--DDLLLEILSRLDPKDLLRLSLVSKRWRSLV 35
FBOX smart00256
A Receptor for Ubiquitination Targets;
22-56 2.08e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 38.19  E-value: 2.08e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 190194416    22 LPWEdvLLPHVLNRVPLRQLLRLQRVSRAFRSLVQ 56
Cdd:smart00256   1 LPDE--ILEEILSKLDPKDLLRLRKVSRKWRSLID 33
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 71-146 5.53e-04

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: 41.21  E-value: 5.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190194416  71 GPQIPRAALARLLRDAEGLQELALAPCHEWLSDEDLVPVLARNPQLRSVALGGCgQLSRRALGALAEGC-PRLQRLS 146
Cdd:cd23951  239 GRSVPKAVLGRVGQHCPRLVELVVCANGNSPIDEELIRIAKNCKQLSSLGLGEC-EVSCSALVEFAKLCgPRLTELY 314
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
165-190 2.77e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.69  E-value: 2.77e-03
                           10        20
                   ....*....|....*....|....*.
gi 190194416   165 CPALEELDLTACRQLKDEAIVYLAQR 190
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 139-266 3.73e-16

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: 75.83  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 139 CPRLQRLSLAHCDWVDGLALRGLADRCPALEELDLTACRQLKDEAIVYLAqRRGAGLRSLSLAVNAN---VGDAAVQELA 215
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALA-TNCPKLQTINLGRHRNghlITDVSLSALG 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 190194416 216 RNCPELHHLDLTGClRVGSDGVRTLAEYC-PVLRSLRVRHCHHVAESSLSRL 266
Cdd:cd09293  130 KNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAI 180
F-box_FBXL15 cd22126
F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also ...
 19-60 3.62e-13

F-box domain found in F-box/LRR-repeat protein 15 (FBXL15) and similar proteins; FBXL15, also called F-box only protein 37 (FBXO37), 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 Smad ubiquitination regulatory factor 1 (SMURF1), thereby acting as a positive regulator of the BMP signaling pathway. It is required for dorsal/ventral pattern formation and bone mass maintenance. It also mediates ubiquitination of SMURF2 and WWP2. 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: 438898  Cd Length: 44  Bit Score: 62.52  E-value: 3.62e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 190194416  19 FLDLPWEDVLLPHVLNRVPLRQLLRLQRVSRAFRSLVQLHLA 60
Cdd:cd22126    1 LLDLPWEDVLFPHILPHLSLKDLFNLRRVSKAFKSLVDEYFS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 164-266 1.26e-12

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: 65.81  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 164 RCPALEELDLTACRQLkDEAIVYLAqrRGAGLRSLSLAVNANVGDAAVQELARNCPELHHLDLTGCLRVGSDGVRTLAEY 243
Cdd:cd09293   26 LHSGLEWLELYMCPIS-DPPLDQLS--NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATN 102

                         90       100
                 ....*....|....*....|....*.
gi 190194416 244 CPVLRSL---RVRHCHHVAESSLSRL 266
Cdd:cd09293  103 CPKLQTInlgRHRNGHLITDVSLSAL 128
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 49-232 3.30e-09

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: 56.18  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416  49 RAFRSLVQLHLAGLRRFDAaQVGPQIPrAALARLLRdAEGLQELALAPCHEwLSDEDLVPVLARNPQLRSVALGGCGQLS 128
Cdd:cd09293   17 SNISQLLRILHSGLEWLEL-YMCPISD-PPLDQLSN-CNKLKKLILPGSKL-IDDEGLIALAQSCPNLQVLDLRACENIT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 129 RRALGALAEGCPRLQRLSLAH---CDWVDGLALRGLADRCPALEELDLTACrQLKDEAIVYLAQRRGAGLRSLSLAVNAN 205
Cdd:cd09293   93 DSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSKSLERLSLNNCRN 171

                        170       180
                 ....*....|....*....|....*....
gi 190194416 206 VGDAAVQEL--ARNCPELHHLDLTGCLRV 232
Cdd:cd09293  172 LTDQSIPAIlaSNYFPNLSVLEFRGCPLI 200
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 28-253 4.61e-05

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.40  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416  28 LLPHVLNRVPLRQLLRLQRVSRAFRSLvqLHLAGLRRFDAAQV-----GPQIPRAALARLLRDAEGLQELALAPCHE--- 99
Cdd:COG5238  133 LYLALPRRINLIQVLKDPLGGNAVHLL--GLAARLGLLAAISMakalqNNSVETVYLGCNQIGDEGIEELAEALTQNttv 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 100 ---WLSD--------EDLVPVLARNPQLRSVALGGcGQLSRRALGALAEGCP---RLQRLSLAHcDWVDGLALRGLAD-- 163
Cdd:COG5238  211 ttlWLKRnpigdegaEILAEALKGNKSLTTLDLSN-NQIGDEGVIALAEALKnntTVETLYLSG-NQIGAEGAIALAKal 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 164 -RCPALEELDLTAcRQLKDEAIVYLAQ--RRGAGLRSLSLAVNaNVGDAAVQELARNC---PELHHLDLTGClRVGSDGV 237
Cdd:COG5238  289 qGNTTLTSLDLSV-NRIGDEGAIALAEglQGNKTLHTLNLAYN-GIGAQGAIALAKALqenTTLHSLDLSDN-QIGDEGA 365

                        250
                 ....*....|....*....
gi 190194416 238 RTLAEY---CPVLRSLRVR 253
Cdd:COG5238  366 IALAKYlegNTTLRELNLG 384
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 19-55 1.90e-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: 38.29  E-value: 1.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 190194416   19 FLDLPweDVLLPHVLNRVPLRQLLRLQRVSRAFRSLV 55
Cdd:pfam00646   1 LLDLP--DDLLLEILSRLDPKDLLRLSLVSKRWRSLV 35
FBOX smart00256
A Receptor for Ubiquitination Targets;
22-56 2.08e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 38.19  E-value: 2.08e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 190194416    22 LPWEdvLLPHVLNRVPLRQLLRLQRVSRAFRSLVQ 56
Cdd:smart00256   1 LPDE--ILEEILSKLDPKDLLRLRKVSRKWRSLID 33
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 71-146 5.53e-04

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: 41.21  E-value: 5.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190194416  71 GPQIPRAALARLLRDAEGLQELALAPCHEWLSDEDLVPVLARNPQLRSVALGGCgQLSRRALGALAEGC-PRLQRLS 146
Cdd:cd23951  239 GRSVPKAVLGRVGQHCPRLVELVVCANGNSPIDEELIRIAKNCKQLSSLGLGEC-EVSCSALVEFAKLCgPRLTELY 314
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
104-228 1.84e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.53  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 104 EDLVPVLARNPQLRSVALGGCgQLSRraLGALAEGCPRLQRLSLAHCDWVD-GLALRGLadrcPALEELDLtACRQLKD- 181
Cdd:COG4886  149 TDLPEPLGNLTNLKSLDLSNN-QLTD--LPEELGNLTNLKELDLSNNQITDlPEPLGNL----TNLEELDL-SGNQLTDl 220

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 190194416 182 -EAIVYLAQrrgagLRSLSLAVNaNVGDaaVQELArNCPELHHLDLTG 228
Cdd:COG4886  221 pEPLANLTN-----LETLDLSNN-QLTD--LPELG-NLTNLEELDLSN 259
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
165-190 2.77e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.69  E-value: 2.77e-03
                           10        20
                   ....*....|....*....|....*.
gi 190194416   165 CPALEELDLTACRQLKDEAIVYLAQR 190
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 128-224 4.01e-03

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: 38.52  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194416 128 SRRALGALAEGCPRLQRLSLAH--CDWVDGlALRGLADRCPALEELDLTACrQLKDEAIVYLAQRRGAGLRSLSLAVNAN 205
Cdd:cd23951  243 PKAVLGRVGQHCPRLVELVVCAngNSPIDE-ELIRIAKNCKQLSSLGLGEC-EVSCSALVEFAKLCGPRLTELYVMEEVL 320

                         90
                 ....*....|....*....
gi 190194416 206 VGDAAVqELARNCPELHHL 224
Cdd:cd23951  321 VEDEEY-DLESATAEVSKY 338
 
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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