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Conserved domains on  [gi|404312677|ref|NP_001258205|]
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F-box/LRR-repeat protein 14 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
F-box_FBXL14 cd22125
F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also ...
6-46 6.99e-26

F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also called F-box and leucine-rich repeat protein 14, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin-protein ligase complex, which acts by mediating ubiquitination and subsequent degradation of SNAIL1. 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: 438897  Cd Length: 41  Bit Score: 98.32  E-value: 6.99e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22125    1 SCLFPEILAMIFSYLDVRDKGRAAQVCTAWRDAAYHKSVWR 41
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
228-395 7.08e-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: 76.21  E-value: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293   28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293  107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185
                        170
                 ....*....|....*..
gi 404312677 380 LPCLKVLNL-GLWQMTD 395
Cdd:cd09293  186 FPNLSVLEFrGCPLITD 202
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
90-296 6.13e-15

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: 73.52  E-value: 6.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677  90 ANIESLNLSGCYNLtDNGLGHafVQEIGSLRALNLSLCKQITDSSLGRIAQYLKGLEVLELGGCSNITNTGLLLIAWGLQ 169
Cdd:cd09293   28 SGLEWLELYMCPIS-DPPLDQ--LSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 170 RLKSLNLRscRHLSdvgiGHLagmtrsaaegclgleqltlqdcqkLTDLSLKHISRGLTGLRLLNLSFCgGISDAGLLHL 249
Cdd:cd09293  105 KLQTINLG--RHRN----GHL------------------------ITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWEL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404312677 250 S--HMGSLRSLNLRSCDNISDTGIMHLAMGSL--RLSGLDVSFCDKVGDQS 296
Cdd:cd09293  154 AsgCSKSLERLSLNNCRNLTDQSIPAILASNYfpNLSVLEFRGCPLITDFS 204
 
Name Accession Description Interval E-value
F-box_FBXL14 cd22125
F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also ...
6-46 6.99e-26

F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also called F-box and leucine-rich repeat protein 14, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin-protein ligase complex, which acts by mediating ubiquitination and subsequent degradation of SNAIL1. 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: 438897  Cd Length: 41  Bit Score: 98.32  E-value: 6.99e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22125    1 SCLFPEILAMIFSYLDVRDKGRAAQVCTAWRDAAYHKSVWR 41
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
228-395 7.08e-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: 76.21  E-value: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293   28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293  107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185
                        170
                 ....*....|....*..
gi 404312677 380 LPCLKVLNL-GLWQMTD 395
Cdd:cd09293  186 FPNLSVLEFrGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
90-296 6.13e-15

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: 73.52  E-value: 6.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677  90 ANIESLNLSGCYNLtDNGLGHafVQEIGSLRALNLSLCKQITDSSLGRIAQYLKGLEVLELGGCSNITNTGLLLIAWGLQ 169
Cdd:cd09293   28 SGLEWLELYMCPIS-DPPLDQ--LSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 170 RLKSLNLRscRHLSdvgiGHLagmtrsaaegclgleqltlqdcqkLTDLSLKHISRGLTGLRLLNLSFCgGISDAGLLHL 249
Cdd:cd09293  105 KLQTINLG--RHRN----GHL------------------------ITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWEL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404312677 250 S--HMGSLRSLNLRSCDNISDTGIMHLAMGSL--RLSGLDVSFCDKVGDQS 296
Cdd:cd09293  154 AsgCSKSLERLSLNNCRNLTDQSIPAILASNYfpNLSVLEFRGCPLITDFS 204
F-box-like pfam12937
F-box-like; This is an F-box-like family.
5-46 1.72e-08

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 50.17  E-value: 1.72e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 404312677    5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
122-400 4.56e-07

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: 51.71  E-value: 4.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 122 LNLSLCKQITDSSLGRIAQ----YLKGLEVLELGGcsniTNTGLLLIAWGLQRLKSLNLRSCRHLSDVGIGHLaGMTRSA 197
Cdd:COG5238  119 LRRIMAKTLEDSLILYLALprriNLIQVLKDPLGG----NAVHLLGLAARLGLLAAISMAKALQNNSVETVYL-GCNQIG 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 198 AEGCLGL-EQLTLQDCQKLTDLSLKHIS-----------RGLTGLRLLNLSFcGGISDAGLL----HLSHMGSLRSLNLr 261
Cdd:COG5238  194 DEGIEELaEALTQNTTVTTLWLKRNPIGdegaeilaealKGNKSLTTLDLSN-NQIGDEGVIalaeALKNNTTVETLYL- 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 262 SCDNISDTGIMHLA---MGSLRLSGLDVSFcDKVGDQSLAYIAQGLDG---LKSLSLCSCHISDDGINRMVRQMHGLRTL 335
Cdd:COG5238  272 SGNQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAQGAIALAKALQENTTL 350
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404312677 336 NIGQCV--RITDKGLELIAEHL---SQLTGIDLyGCTRITKRGLERIT---QLPCLKVLNLGLWQMTDSEKVR 400
Cdd:COG5238  351 HSLDLSdnQIGDEGAIALAKYLegnTTLRELNL-GKNNIGKQGAEALIdalQTNRLHTLILDGNLIGAEAQQR 422
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-268 9.88e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.70  E-value: 9.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677  74 QILSLRRSLSYVIQGMANIESLNLSGCyNLTDngLGHAFVQeIGSLRALNLSLCkQITD--SSLGRiaqyLKGLEVLELG 151
Cdd:COG4886   97 NLTELDLSGNEELSNLTNLESLDLSGN-QLTD--LPEELAN-LTNLKELDLSNN-QLTDlpEPLGN----LTNLKSLDLS 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 152 GCsNITNTGLLLiaWGLQRLKSLNLRSCRhLSDVGiGHLAGMTRsaaegclgLEQLTLQDCQkLTDLSLKhISRgLTGLR 231
Cdd:COG4886  168 NN-QLTDLPEEL--GNLTNLKELDLSNNQ-ITDLP-EPLGNLTN--------LEELDLSGNQ-LTDLPEP-LAN-LTNLE 231
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 404312677 232 LLNLSFCgGISDagLLHLSHMGSLRSLNLRSCdNISD 268
Cdd:COG4886  232 TLDLSNN-QLTD--LPELGNLTNLEELDLSNN-QLTD 264
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
252-275 6.54e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 33.92  E-value: 6.54e-03
                           10        20
                   ....*....|....*....|....
gi 404312677   252 MGSLRSLNLRSCDNISDTGIMHLA 275
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
FBOX smart00256
A Receptor for Ubiquitination Targets;
8-46 9.34e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 33.95  E-value: 9.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 404312677     8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
 
Name Accession Description Interval E-value
F-box_FBXL14 cd22125
F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also ...
6-46 6.99e-26

F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also called F-box and leucine-rich repeat protein 14, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin-protein ligase complex, which acts by mediating ubiquitination and subsequent degradation of SNAIL1. 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: 438897  Cd Length: 41  Bit Score: 98.32  E-value: 6.99e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22125    1 SCLFPEILAMIFSYLDVRDKGRAAQVCTAWRDAAYHKSVWR 41
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
228-395 7.08e-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: 76.21  E-value: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293   28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293  107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185
                        170
                 ....*....|....*..
gi 404312677 380 LPCLKVLNL-GLWQMTD 395
Cdd:cd09293  186 FPNLSVLEFrGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
90-296 6.13e-15

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: 73.52  E-value: 6.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677  90 ANIESLNLSGCYNLtDNGLGHafVQEIGSLRALNLSLCKQITDSSLGRIAQYLKGLEVLELGGCSNITNTGLLLIAWGLQ 169
Cdd:cd09293   28 SGLEWLELYMCPIS-DPPLDQ--LSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 170 RLKSLNLRscRHLSdvgiGHLagmtrsaaegclgleqltlqdcqkLTDLSLKHISRGLTGLRLLNLSFCgGISDAGLLHL 249
Cdd:cd09293  105 KLQTINLG--RHRN----GHL------------------------ITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWEL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404312677 250 S--HMGSLRSLNLRSCDNISDTGIMHLAMGSL--RLSGLDVSFCDKVGDQS 296
Cdd:cd09293  154 AsgCSKSLERLSLNNCRNLTDQSIPAILASNYfpNLSVLEFRGCPLITDFS 204
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
82-219 1.95e-10

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 60.42  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677  82 LSYVIQGMANIESLNLSGCYNLTDNGLgHAFVQEIGSLRALNLSL---CKQITDSSLGRIAQYLKGLEVLELGGCsNITN 158
Cdd:cd09293   70 LIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404312677 159 TGLLLIAWG-LQRLKSLNLRSCRHLSDVGIGHLAGMTrsaaeGCLGLEQLTLQDCQKLTDLS 219
Cdd:cd09293  148 KGVWELASGcSKSLERLSLNNCRNLTDQSIPAILASN-----YFPNLSVLEFRGCPLITDFS 204
F-box-like pfam12937
F-box-like; This is an F-box-like family.
5-46 1.72e-08

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 50.17  E-value: 1.72e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 404312677    5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
6-39 5.08e-08

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: 48.51  E-value: 5.08e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 404312677   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAA 39
Cdd:cd22121    1 NALPEEILVHIFRHLSLRDRYAAAQVCKHWREAA 34
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
11-46 1.68e-07

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: 47.25  E-value: 1.68e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 404312677  11 ELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22104    7 VVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWR 42
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
122-400 4.56e-07

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: 51.71  E-value: 4.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 122 LNLSLCKQITDSSLGRIAQ----YLKGLEVLELGGcsniTNTGLLLIAWGLQRLKSLNLRSCRHLSDVGIGHLaGMTRSA 197
Cdd:COG5238  119 LRRIMAKTLEDSLILYLALprriNLIQVLKDPLGG----NAVHLLGLAARLGLLAAISMAKALQNNSVETVYL-GCNQIG 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 198 AEGCLGL-EQLTLQDCQKLTDLSLKHIS-----------RGLTGLRLLNLSFcGGISDAGLL----HLSHMGSLRSLNLr 261
Cdd:COG5238  194 DEGIEELaEALTQNTTVTTLWLKRNPIGdegaeilaealKGNKSLTTLDLSN-NQIGDEGVIalaeALKNNTTVETLYL- 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 262 SCDNISDTGIMHLA---MGSLRLSGLDVSFcDKVGDQSLAYIAQGLDG---LKSLSLCSCHISDDGINRMVRQMHGLRTL 335
Cdd:COG5238  272 SGNQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAQGAIALAKALQENTTL 350
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404312677 336 NIGQCV--RITDKGLELIAEHL---SQLTGIDLyGCTRITKRGLERIT---QLPCLKVLNLGLWQMTDSEKVR 400
Cdd:COG5238  351 HSLDLSdnQIGDEGAIALAKYLegnTTLRELNL-GKNNIGKQGAEALIdalQTNRLHTLILDGNLIGAEAQQR 422
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-268 9.88e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.70  E-value: 9.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677  74 QILSLRRSLSYVIQGMANIESLNLSGCyNLTDngLGHAFVQeIGSLRALNLSLCkQITD--SSLGRiaqyLKGLEVLELG 151
Cdd:COG4886   97 NLTELDLSGNEELSNLTNLESLDLSGN-QLTD--LPEELAN-LTNLKELDLSNN-QLTDlpEPLGN----LTNLKSLDLS 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 152 GCsNITNTGLLLiaWGLQRLKSLNLRSCRhLSDVGiGHLAGMTRsaaegclgLEQLTLQDCQkLTDLSLKhISRgLTGLR 231
Cdd:COG4886  168 NN-QLTDLPEEL--GNLTNLKELDLSNNQ-ITDLP-EPLGNLTN--------LEELDLSGNQ-LTDLPEP-LAN-LTNLE 231
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 404312677 232 LLNLSFCgGISDagLLHLSHMGSLRSLNLRSCdNISD 268
Cdd:COG4886  232 TLDLSNN-QLTD--LPELGNLTNLEELDLSNN-QLTD 264
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
11-48 1.49e-06

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. 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: 438881  Cd Length: 47  Bit Score: 44.63  E-value: 1.49e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 404312677  11 ELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRGV 48
Cdd:cd22109    9 DALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRV 46
F-box_FBXL16 cd22127
F-box domain found in F-box/LRR-repeat protein 16 (FBXL16) and similar proteins; FBXL16, also ...
7-47 2.09e-06

F-box domain found in F-box/LRR-repeat protein 16 (FBXL16) and similar proteins; FBXL16, also called F-box and leucine-rich repeat protein 16, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a repressor of one of the earliest steps in the cardiogenic lineage: FLK1+ progenitor formation. 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: 438899  Cd Length: 42  Bit Score: 44.23  E-value: 2.09e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   7 CLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRG 47
Cdd:cd22127    2 LLDEKFLNRLFWYFSPCERCVLAQVCKKWRDVLYQPKFWRG 42
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
113-310 6.54e-06

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: 47.86  E-value: 6.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 113 VQEIGSLRALNLSLcKQITDSSLGRIAQYLKG---LEVLELGGcSNITNTGLLLIAWGLQRLKslNLRSCrHLSDVGIGh 189
Cdd:COG5238  232 LKGNKSLTTLDLSN-NQIGDEGVIALAEALKNnttVETLYLSG-NQIGAEGAIALAKALQGNT--TLTSL-DLSVNRIG- 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 190 lagmtrsaAEGCLGLEQlTLQDCQKLTDLSLKHISRGLTGLRLL-----------NLSFCGG-ISDAGLLHLSH----MG 253
Cdd:COG5238  306 --------DEGAIALAE-GLQGNKTLHTLNLAYNGIGAQGAIALakalqenttlhSLDLSDNqIGDEGAIALAKylegNT 376
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 404312677 254 SLRSLNLRScDNISDTGIMHLAMGSL--RLSGLDVSFCDkVGDQSLAYIAQGLDGLKSL 310
Cdd:COG5238  377 TLRELNLGK-NNIGKQGAEALIDALQtnRLHTLILDGNL-IGAEAQQRLEQLLERIKSV 433
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
6-40 8.58e-06

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: 42.05  E-value: 8.58e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 404312677   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAY 40
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
5-45 8.88e-06

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. 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: 438890  Cd Length: 41  Bit Score: 42.33  E-value: 8.88e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22118    1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
5-46 4.88e-05

F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also called F-box and leucine-rich repeat protein 12, or F-box protein FBL12, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the polyubiquitination and proteasomal degradation of calcium/calmodulin dependent protein kinase I (CAMK1) leading to disruption of cyclin D1/CDK4 complex assembly, which results in G1 cell cycle arrest in lung epithelia. It regulates T-cell differentiation in a cell-autonomous manner. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438895  Cd Length: 42  Bit Score: 40.41  E-value: 4.88e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 404312677   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22123    1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42
F-box_FBXO31 cd22102
F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called ...
8-46 5.73e-05

F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called FBX31, or FBXO14, is a component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. It specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest. FBXO31 may act as a tumor suppressor. 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: 438874  Cd Length: 48  Bit Score: 40.10  E-value: 5.73e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 404312677   8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22102    4 LPPELLVEIFSSLPGTDLPSLAQVCKKFREILNTDTIWQ 42
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
6-46 5.80e-05

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. 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: 438922  Cd Length: 44  Bit Score: 40.00  E-value: 5.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22151    1 RKLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWE 41
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
5-37 8.17e-05

F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called FBX48, is one of the paralogs of the F-box only protein 7 (FBXO7), which is the causative gene for PARK15 (also known as Parkinsonian-pyramidal disease, PPD). 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: 438885  Cd Length: 46  Bit Score: 39.61  E-value: 8.17e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 404312677   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRD 37
Cdd:cd22113    1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWND 33
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
10-46 1.03e-04

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), 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: 438891  Cd Length: 47  Bit Score: 39.54  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 404312677  10 PELLAMIFGYLdVRDKG------RAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22119    6 PEILVKIFQFA-VATEGavpllcRLSRVCRLWREVALDPSLWT 47
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
4-37 1.06e-04

F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called FBX10, or PRMT11, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an anti-apoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. It also associates with the receptor for advanced glycation end products (RAGE) to mediate its ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438862  Cd Length: 50  Bit Score: 39.64  E-value: 1.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 404312677   4 HISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRD 37
Cdd:cd22090    1 EVTGLPLELWRLILAYLPVRDLCRCCQVCRAWYE 34
F-box_FBXO39 cd22108
F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called ...
10-46 1.31e-04

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: 39.32  E-value: 1.31e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 404312677  10 PEL-LAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22108    5 PDVcLRHVFRWLGDRDRSRAALVCKRWNQAMYSPALWR 42
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
5-46 1.73e-04

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. 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: 438918  Cd Length: 46  Bit Score: 38.83  E-value: 1.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 404312677   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22147    2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWK 43
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
5-45 4.33e-04

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also 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: 438896  Cd Length: 42  Bit Score: 37.70  E-value: 4.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
202-388 4.66e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 42.23  E-value: 4.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 202 LGLEQLTLQDCQKLTDLSLKHISRGLTGLRLLNLSFCGGISdagllhlsHMGSLRSLNLRSCdNISDTGImhlAMGSLR- 280
Cdd:COG4886   70 SLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS--------NLTNLESLDLSGN-QLTDLPE---ELANLTn 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404312677 281 LSGLDVSFCdKVGDQSlAYIAQgLDGLKSLSLCSCHISDdgINRMVRQMHGLRTLNIGQCvRITDKGLELiaEHLSQLTG 360
Cdd:COG4886  138 LKELDLSNN-QLTDLP-EPLGN-LTNLKSLDLSNNQLTD--LPEELGNLTNLKELDLSNN-QITDLPEPL--GNLTNLEE 209
                        170       180
                 ....*....|....*....|....*...
gi 404312677 361 IDLYGcTRITKRGLErITQLPCLKVLNL 388
Cdd:COG4886  210 LDLSG-NQLTDLPEP-LANLTNLETLDL 235
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
5-46 5.70e-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: 37.13  E-value: 5.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 404312677    5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
8-46 2.18e-03

F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar proteins; The family includes FBXL2 and FBXL30. FBXL2, also called F-box and leucine-rich repeat protein 2, or F-box protein FBL2/FBL3, is a calcium-activated substrate-recognition component of an SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. FBXL20, also called SCRAPPER, F-box and leucine-rich repeat protein 20, or F-box/LRR-repeat protein 2-like, is a component of a synapse-localized SCF-type E3 ubiquitin ligase which regulates neural transmission. It is widely expressed in the central nervous system and plays an important role in the ubiquitin-dependent degradation of regulating synaptic membrane exocytosis 1 (RIM1), which is an important factor in the release of synaptic vesicles. It may also mediate the ubiquitin degradation of E-cadherin resulting in an increased invasive ability of malignant cells. 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: 438887  Cd Length: 45  Bit Score: 35.86  E-value: 2.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 404312677   8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22115    7 LPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45
F-box_FBXL3 cd22178
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also ...
8-45 2.24e-03

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also called F-box and leucine-rich repeat protein 3A, or F-box/LRR-repeat protein 3A, is the substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex that mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2, and thus, is involved in circadian rhythm function. It plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. 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: 438949  Cd Length: 43  Bit Score: 35.65  E-value: 2.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 404312677   8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22178    6 LLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
6-45 3.34e-03

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438886  Cd Length: 41  Bit Score: 35.08  E-value: 3.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 404312677   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22114    2 DSLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41
F-box_ECT2L cd22173
F-box domain found in epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and ...
8-47 3.83e-03

F-box domain found in epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). 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: 438944  Cd Length: 52  Bit Score: 35.08  E-value: 3.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 404312677   8 LFPELLAM-IFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRG 47
Cdd:cd22173    5 VLPRFLSLyIFSFLDPRSLCRAAQVSWHWKFLAEQDCLWMP 45
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
7-45 4.05e-03

F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, also called F-box and WD-40 domain-containing protein 8, or F-box only protein 29 (FBXO29), is the substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as GORASP1, IRS1, MAP4K1/HPK1. 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: 438906  Cd Length: 48  Bit Score: 35.04  E-value: 4.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 404312677   7 CLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22134    6 QLPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLW 44
F-box_FBXW7 cd22133
F-box domain found in F-box/WD repeat-containing protein 7 (FBXW7) and similar proteins; FBXW7, ...
5-46 6.08e-03

F-box domain found in F-box/WD repeat-containing protein 7 (FBXW7) and similar proteins; FBXW7, also called Archipelago homolog (Ago), F-box and WD-40 domain-containing protein 7, F-box protein FBX30, SEL-10, or Cdc4, 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, such as cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, and probably PSEN1. 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: 438905  Cd Length: 59  Bit Score: 34.71  E-value: 6.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 404312677   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22133   18 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
252-275 6.54e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 33.92  E-value: 6.54e-03
                           10        20
                   ....*....|....*....|....
gi 404312677   252 MGSLRSLNLRSCDNISDTGIMHLA 275
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
F-box_FBXO16-like cd22094
F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 ...
9-45 6.67e-03

F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; This family includes FBXO16 and ECT2L. FBXO16, also called FBX16, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It functions as a tumor suppressor by attenuating nuclear beta-catenin function. ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). 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: 438866  Cd Length: 49  Bit Score: 34.34  E-value: 6.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 404312677   9 FPELLAM-IFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22094    6 LPRFLSLyIFSYLDPRSLCRAAQVSWYWKFLCESDELW 43
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
16-48 8.10e-03

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). 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: 438910  Cd Length: 45  Bit Score: 34.23  E-value: 8.10e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 404312677  16 IFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRGV 48
Cdd:cd22138   12 IFSFLSEVDKCLAATVCRSWSELIRSPRLWRTV 44
FBOX smart00256
A Receptor for Ubiquitination Targets;
8-46 9.34e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 33.95  E-value: 9.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 404312677     8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
 
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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