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Conserved domains on  [gi|17647819|ref|NP_523812|]
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partner of paired, isoform A [Drosophila melanogaster]

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 ...
150-190 2.12e-21

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: 87.15  E-value: 2.12e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22125   1 SCLFPEILAMIFSYLDVRDKGRAAQVCTAWRDAAYHKSVWR 41
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
347-524 2.52e-19

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: 87.00  E-value: 2.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 347 QLEYLGLQDCQRlSDEALGHIAQGlTSLKSINLSFCVSVTDSGLKHLAR-MPKLEQLNLRSCDNISDIGMAYLTEGGSGI 425
Cdd:cd09293  29 GLEWLELYMCPI-SDPPLDQLSNC-NKLKKLILPGSKLIDDEGLIALAQsCPNLQVLDLRACENITDSGIVALATNCPKL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 426 NSLDVSF---CDKISDQALTHIAQGLYRLRSLSLNQCQITDHGMLKIA-KALHELENLNIGQCSRITDKGL-QTLAEDLT 500
Cdd:cd09293 107 QTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsGCSKSLERLSLNNCRNLTDQSIpAILASNYF 186
                       170       180
                ....*....|....*....|....*
gi 17647819 501 -NLKTIDLYGCTQLSSKGIDIIMKL 524
Cdd:cd09293 187 pNLSVLEFRGCPLITDFSRIILFKL 211
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
226-334 4.93e-11

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: 62.73  E-value: 4.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 226 LKDLVLGVPALTSLNLSGCFNVADMNLgHAFSVDLPNLKTLDLSL---CKQITDTSLGRIAQHLRNLETLELGGcCNITN 302
Cdd:cd09293  70 LIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAG-CDVTD 147
                        90       100       110
                ....*....|....*....|....*....|...
gi 17647819 303 TGLLLIAWG-LKKLKHLNLRSCWHISDQGIGHL 334
Cdd:cd09293 148 KGVWELASGcSKSLERLSLNNCRNLTDQSIPAI 180
 
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 ...
150-190 2.12e-21

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: 87.15  E-value: 2.12e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22125   1 SCLFPEILAMIFSYLDVRDKGRAAQVCTAWRDAAYHKSVWR 41
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
347-524 2.52e-19

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: 87.00  E-value: 2.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 347 QLEYLGLQDCQRlSDEALGHIAQGlTSLKSINLSFCVSVTDSGLKHLAR-MPKLEQLNLRSCDNISDIGMAYLTEGGSGI 425
Cdd:cd09293  29 GLEWLELYMCPI-SDPPLDQLSNC-NKLKKLILPGSKLIDDEGLIALAQsCPNLQVLDLRACENITDSGIVALATNCPKL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 426 NSLDVSF---CDKISDQALTHIAQGLYRLRSLSLNQCQITDHGMLKIA-KALHELENLNIGQCSRITDKGL-QTLAEDLT 500
Cdd:cd09293 107 QTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsGCSKSLERLSLNNCRNLTDQSIpAILASNYF 186
                       170       180
                ....*....|....*....|....*
gi 17647819 501 -NLKTIDLYGCTQLSSKGIDIIMKL 524
Cdd:cd09293 187 pNLSVLEFRGCPLITDFSRIILFKL 211
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
322-538 1.16e-11

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: 66.74  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 322 SCWHISDQGIGHLAgfsrETAEGNLQLEYLGLQDCQ--RLSDEALGHIAQGLTSLKSINLSFcVSVTDSGL----KHLAR 395
Cdd:COG5238 188 GCNQIGDEGIEELA----EALTQNTTVTTLWLKRNPigDEGAEILAEALKGNKSLTTLDLSN-NQIGDEGVialaEALKN 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 396 MPKLEQLNLrSCDNISDIGMAYLTE---GGSGINSLDVSFcDKISDQALTHIAQGLYR---LRSLSLNQCQITDHGMLKI 469
Cdd:COG5238 263 NTTVETLYL-SGNQIGAEGAIALAKalqGNTTLTSLDLSV-NRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAQGAIAL 340
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647819 470 AKALHE---LENLNIgQCSRITDKGLQTLAEDL---TNLKTIDLyGCTQLSSKGIDII---MKLPKLQKLNLGLWLVR 538
Cdd:COG5238 341 AKALQEnttLHSLDL-SDNQIGDEGAIALAKYLegnTTLRELNL-GKNNIGKQGAEALidaLQTNRLHTLILDGNLIG 416
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
226-334 4.93e-11

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: 62.73  E-value: 4.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 226 LKDLVLGVPALTSLNLSGCFNVADMNLgHAFSVDLPNLKTLDLSL---CKQITDTSLGRIAQHLRNLETLELGGcCNITN 302
Cdd:cd09293  70 LIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAG-CDVTD 147
                        90       100       110
                ....*....|....*....|....*....|...
gi 17647819 303 TGLLLIAWG-LKKLKHLNLRSCWHISDQGIGHL 334
Cdd:cd09293 148 KGVWELASGcSKSLERLSLNNCRNLTDQSIPAI 180
F-box-like pfam12937
F-box-like; This is an F-box-like family.
149-190 2.15e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 52.87  E-value: 2.15e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 17647819   149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
226-501 2.35e-07

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 53.73  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819   226 LKDLVLGVPALTSL---NLSGCFNVADM-NLGHAfsvdlPNLKTLDLSLCKQITDTSLGriAQHLRNLETLELGGCCNIT 301
Cdd:PLN03210  623 LEKLWDGVHSLTGLrniDLRGSKNLKEIpDLSMA-----TNLETLKLSDCSSLVELPSS--IQYLNKLEDLDMSRCENLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819   302 NtglLLIAWGLKKLKHLNLRSCWHI-------SDQGIGHLAGFSRETAEGNLQLEYLGLQDCQRLSDEALGHIAQGLTSL 374
Cdd:PLN03210  696 I---LPTGINLKSLYRLNLSGCSRLksfpdisTNISWLDLDETAIEEFPSNLRLENLDELILCEMKSEKLWERVQPLTPL 772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819   375 KSINLSFCVSVTDSGLKHLARMP-------KLEQLNLRSCDNISDIgmayltegGSGIN-----SLDVSFCDK------- 435
Cdd:PLN03210  773 MTMLSPSLTRLFLSDIPSLVELPssiqnlhKLEHLEIENCINLETL--------PTGINlesleSLDLSGCSRlrtfpdi 844
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647819   436 ---ISDQALTHIA--------QGLYRLRSLSLNQCQITDHGMLKIAKaLHELENLNIGQCSRITDKGLQTLAEDLTN 501
Cdd:PLN03210  845 stnISDLNLSRTGieevpwwiEKFSNLSFLDMNGCNNLQRVSLNISK-LKHLETVDFSDCGALTEASWNGSPSEVAM 920
FBOX smart00256
A Receptor for Ubiquitination Targets;
152-190 2.20e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 2.20e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17647819    152 LFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
473-496 6.77e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 6.77e-03
                           10        20
                   ....*....|....*....|....
gi 17647819    473 LHELENLNIGQCSRITDKGLQTLA 496
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
 
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 ...
150-190 2.12e-21

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: 87.15  E-value: 2.12e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22125   1 SCLFPEILAMIFSYLDVRDKGRAAQVCTAWRDAAYHKSVWR 41
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
347-524 2.52e-19

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: 87.00  E-value: 2.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 347 QLEYLGLQDCQRlSDEALGHIAQGlTSLKSINLSFCVSVTDSGLKHLAR-MPKLEQLNLRSCDNISDIGMAYLTEGGSGI 425
Cdd:cd09293  29 GLEWLELYMCPI-SDPPLDQLSNC-NKLKKLILPGSKLIDDEGLIALAQsCPNLQVLDLRACENITDSGIVALATNCPKL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 426 NSLDVSF---CDKISDQALTHIAQGLYRLRSLSLNQCQITDHGMLKIA-KALHELENLNIGQCSRITDKGL-QTLAEDLT 500
Cdd:cd09293 107 QTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsGCSKSLERLSLNNCRNLTDQSIpAILASNYF 186
                       170       180
                ....*....|....*....|....*
gi 17647819 501 -NLKTIDLYGCTQLSSKGIDIIMKL 524
Cdd:cd09293 187 pNLSVLEFRGCPLITDFSRIILFKL 211
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
237-457 4.35e-19

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: 86.23  E-value: 4.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 237 TSLNLSGCFNVADMNLGHAFSVDLPNLKTLDLSLCKQItDTSLGRIaQHLRNLETLELGGCCNITNTGLLLIAWGLKKLK 316
Cdd:cd09293   4 LLFILHKLGQITQSNISQLLRILHSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 317 HLNLRSCWHISDQGIGHLAGFSRetaegNLQLEYLGL-QDCQRLSDEALGHIAQGLTSLKSINLSFCvSVTDSGLKHLAR 395
Cdd:cd09293  82 VLDLRACENITDSGIVALATNCP-----KLQTINLGRhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELAS 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647819 396 M--PKLEQLNLRSCDNISDIGMAYLTEGGS--GINSLDVSFCDKISDqaLTHIAqgLYRLRSLSLN 457
Cdd:cd09293 156 GcsKSLERLSLNNCRNLTDQSIPAILASNYfpNLSVLEFRGCPLITD--FSRII--LFKLWQPRLN 217
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
322-538 1.16e-11

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: 66.74  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 322 SCWHISDQGIGHLAgfsrETAEGNLQLEYLGLQDCQ--RLSDEALGHIAQGLTSLKSINLSFcVSVTDSGL----KHLAR 395
Cdd:COG5238 188 GCNQIGDEGIEELA----EALTQNTTVTTLWLKRNPigDEGAEILAEALKGNKSLTTLDLSN-NQIGDEGVialaEALKN 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 396 MPKLEQLNLrSCDNISDIGMAYLTE---GGSGINSLDVSFcDKISDQALTHIAQGLYR---LRSLSLNQCQITDHGMLKI 469
Cdd:COG5238 263 NTTVETLYL-SGNQIGAEGAIALAKalqGNTTLTSLDLSV-NRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAQGAIAL 340
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647819 470 AKALHE---LENLNIgQCSRITDKGLQTLAEDL---TNLKTIDLyGCTQLSSKGIDII---MKLPKLQKLNLGLWLVR 538
Cdd:COG5238 341 AKALQEnttLHSLDL-SDNQIGDEGAIALAKYLegnTTLRELNL-GKNNIGKQGAEALidaLQTNRLHTLILDGNLIG 416
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
226-334 4.93e-11

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: 62.73  E-value: 4.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 226 LKDLVLGVPALTSLNLSGCFNVADMNLgHAFSVDLPNLKTLDLSL---CKQITDTSLGRIAQHLRNLETLELGGcCNITN 302
Cdd:cd09293  70 LIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAG-CDVTD 147
                        90       100       110
                ....*....|....*....|....*....|...
gi 17647819 303 TGLLLIAWG-LKKLKHLNLRSCWHISDQGIGHL 334
Cdd:cd09293 148 KGVWELASGcSKSLERLSLNNCRNLTDQSIPAI 180
F-box-like pfam12937
F-box-like; This is an F-box-like family.
149-190 2.15e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 52.87  E-value: 2.15e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 17647819   149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
181-532 3.09e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.18  E-value: 3.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 181 DAAYAKSVWKGVEAKLHLKRSSPSLFNCLVKRGIKKVQILSLRRSLKDLVLGVPALTSLNLSGCFNVADMNLGHAFSVDL 260
Cdd:COG4886  16 LLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 261 PNLKTLDLSLCKQITdtslgriaqHLRNLETLELGGCcNITNTGLLLiaWGLKKLKHLNLRSCwHISD--QGIGHLAgfs 338
Cdd:COG4886  96 TNLTELDLSGNEELS---------NLTNLESLDLSGN-QLTDLPEEL--ANLTNLKELDLSNN-QLTDlpEPLGNLT--- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 339 retaegnlQLEYLGLQDCQrLSDeaLGHIAQGLTSLKSINLSFCvSVTDSGlKHLARMPKLEQLNLRSCdNISDIG--MA 416
Cdd:COG4886 160 --------NLKSLDLSNNQ-LTD--LPEELGNLTNLKELDLSNN-QITDLP-EPLGNLTNLEELDLSGN-QLTDLPepLA 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 417 YLTEggsgINSLDVSFCdKISDqaLTHIAQgLYRLRSLSLNQCQITDhgmLKIAKALHELENLNIgQCSRITDKGLQTLA 496
Cdd:COG4886 226 NLTN----LETLDLSNN-QLTD--LPELGN-LTNLEELDLSNNQLTD---LPPLANLTNLKTLDL-SNNQLTDLKLKELE 293
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 17647819 497 EDLTNLKTIDLYGCTQLSSKGIDIIMKLPKLQKLNL 532
Cdd:COG4886 294 LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLL 329
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
260-505 6.70e-08

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: 54.28  E-value: 6.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 260 LPNLKTLDLSLCkQITDTSLGRIAQHLR-NLETLELGGCCNIT---NTGLLLIAWGLKK---LKHLNLRSCwHISDQGIG 332
Cdd:cd00116  22 LLCLQVLRLEGN-TLGEEAAKALASALRpQPSLKELCLSLNETgriPRGLQSLLQGLTKgcgLQELDLSDN-ALGPDGCG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 333 HLAGFSRETAEGNLQLEylglqDCqRLSDEALGHIAQGLTS----LKSINLSFCvSVTDSGLKHLAR----MPKLEQLNL 404
Cdd:cd00116 100 VLESLLRSSSLQELKLN-----NN-GLGDRGLRLLAKGLKDlppaLEKLVLGRN-RLEGASCEALAKalraNRDLKELNL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 405 RScDNISDIGMAYLTEGGSGINSLDV-----SFCDKISDQALTHIAQGLYRLRSLSLNQCQITDHGMLKIAKAL----HE 475
Cdd:cd00116 173 AN-NGIGDAGIRALAEGLKANCNLEVldlnnNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALlspnIS 251
                       250       260       270
                ....*....|....*....|....*....|
gi 17647819 476 LENLNIGQCSrITDKGLQTLAEDLTNLKTI 505
Cdd:cd00116 252 LLTLSLSCND-ITDDGAKDLAEVLAEKESL 280
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
150-190 1.21e-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: 48.02  E-value: 1.21e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22104   2 ANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWR 42
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
150-184 2.11e-07

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: 47.05  E-value: 2.11e-07
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAY 184
Cdd:cd09917   1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
226-501 2.35e-07

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 53.73  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819   226 LKDLVLGVPALTSL---NLSGCFNVADM-NLGHAfsvdlPNLKTLDLSLCKQITDTSLGriAQHLRNLETLELGGCCNIT 301
Cdd:PLN03210  623 LEKLWDGVHSLTGLrniDLRGSKNLKEIpDLSMA-----TNLETLKLSDCSSLVELPSS--IQYLNKLEDLDMSRCENLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819   302 NtglLLIAWGLKKLKHLNLRSCWHI-------SDQGIGHLAGFSRETAEGNLQLEYLGLQDCQRLSDEALGHIAQGLTSL 374
Cdd:PLN03210  696 I---LPTGINLKSLYRLNLSGCSRLksfpdisTNISWLDLDETAIEEFPSNLRLENLDELILCEMKSEKLWERVQPLTPL 772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819   375 KSINLSFCVSVTDSGLKHLARMP-------KLEQLNLRSCDNISDIgmayltegGSGIN-----SLDVSFCDK------- 435
Cdd:PLN03210  773 MTMLSPSLTRLFLSDIPSLVELPssiqnlhKLEHLEIENCINLETL--------PTGINlesleSLDLSGCSRlrtfpdi 844
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647819   436 ---ISDQALTHIA--------QGLYRLRSLSLNQCQITDHGMLKIAKaLHELENLNIGQCSRITDKGLQTLAEDLTN 501
Cdd:PLN03210  845 stnISDLNLSRTGieevpwwiEKFSNLSFLDMNGCNNLQRVSLNISK-LKHLETVDFSDCGALTEASWNGSPSEVAM 920
F-box_FBXO31 cd22102
F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called ...
149-190 3.77e-07

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: 46.65  E-value: 3.77e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17647819 149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22102   1 ILDLPPELLVEIFSSLPGTDLPSLAQVCKKFREILNTDTIWQ 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
450-533 5.76e-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: 50.40  E-value: 5.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 450 RLRSLSLNQCQITDhGMLKIAKALHELENLNIGQCSRITDKGLQTLAEDLTNLKTIDLYGCTQLSSKGI-DIIMKLPKLQ 528
Cdd:cd09293  29 GLEWLELYMCPISD-PPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIvALATNCPKLQ 107

                ....*
gi 17647819 529 KLNLG 533
Cdd:cd09293 108 TINLG 112
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
352-533 8.56e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.47  E-value: 8.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 352 GLQDCQRLSDEALGHIAQgLTSLKSINLSFCvSVTDSGlKHLARMPKLEQLNLRSCdNISDIG--MAYLTEggsgINSLD 429
Cdd:COG4886  94 DLTNLTELDLSGNEELSN-LTNLESLDLSGN-QLTDLP-EELANLTNLKELDLSNN-QLTDLPepLGNLTN----LKSLD 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 430 VSFCdKISDqaLTHIAQGLYRLRSLSLNQCQITDhgmlkIAKALHELENLNIGQCSritDKGLQTLAED---LTNLKTID 506
Cdd:COG4886 166 LSNN-QLTD--LPEELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLS---GNQLTDLPEPlanLTNLETLD 234
                       170       180
                ....*....|....*....|....*..
gi 17647819 507 LYGcTQLSSkgIDIIMKLPKLQKLNLG 533
Cdd:COG4886 235 LSN-NQLTD--LPELGNLTNLEELDLS 258
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
151-190 9.44e-07

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: 45.42  E-value: 9.44e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647819 151 NLFPE-LLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22123   2 DQLPEnVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
149-190 1.39e-06

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: 45.32  E-value: 1.39e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17647819 149 ISNLFPELLEQIFEHL-----PVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22119   1 GQRLPPEILVKIFQFAvategAVPLLCRLSRVCRLWREVALDPSLWT 47
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
236-536 1.55e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.70  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 236 LTSLNLSGCFNVADmnlghafsvdLPNLKTLDLSlCKQITDtsLGRIAQHLRNLETLELGGCcNITNTGLLLiaWGLKKL 315
Cdd:COG4886  98 LTELDLSGNEELSN----------LTNLESLDLS-GNQLTD--LPEELANLTNLKELDLSNN-QLTDLPEPL--GNLTNL 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 316 KHLNLRSCwHISD--QGIGHLAgfsretaegnlQLEYLGLQDCQrLSD--EALGhiaqGLTSLKSINLSfcvsvtDSGLK 391
Cdd:COG4886 162 KSLDLSNN-QLTDlpEELGNLT-----------NLKELDLSNNQ-ITDlpEPLG----NLTNLEELDLS------GNQLT 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 392 HL----ARMPKLEQLNLRSCdNISDI-GMAYLTEggsgINSLDVSFCdKISDqaLTHIAQgLYRLRSLSLNQCQITDHGM 466
Cdd:COG4886 219 DLpeplANLTNLETLDLSNN-QLTDLpELGNLTN----LEELDLSNN-QLTD--LPPLAN-LTNLKTLDLSNNQLTDLKL 289
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 467 LKIAKALHELENLNIGQCSRITDKGLQTLAEDLTNLKTIDLYGCTQLSSKGIDIIMKLPKLQKLNLGLWL 536
Cdd:COG4886 290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLL 359
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
149-189 2.88e-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: 44.25  E-value: 2.88e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647819 149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVW 189
Cdd:cd22118   1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
149-190 3.73e-06

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: 43.68  E-value: 3.73e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 17647819   149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
148-181 4.18e-06

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: 43.88  E-value: 4.18e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 17647819 148 HISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRD 181
Cdd:cd22090   1 EVTGLPLELWRLILAYLPVRDLCRCCQVCRAWYE 34
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
154-183 4.74e-06

F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also called F-box and leucine-rich repeat protein 8, or F-box protein FBL8, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438893  Cd Length: 35  Bit Score: 43.50  E-value: 4.74e-06
                        10        20        30
                ....*....|....*....|....*....|
gi 17647819 154 PELLEQIFEHLPVRDLGRAAQVCTAWRDAA 183
Cdd:cd22121   5 EEILVHIFRHLSLRDRYAAAQVCKHWREAA 34
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
155-189 5.24e-06

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: 43.46  E-value: 5.24e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17647819 155 ELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVW 189
Cdd:cd22151   6 DLLQEIFKRLDPKSLARAACVCRRWRAAARSESLW 40
FBOX smart00256
A Receptor for Ubiquitination Targets;
152-190 2.20e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 2.20e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17647819    152 LFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
F-box_FBXO22 cd22097
F-box domain found in F-box only protein 22 (FBXO22) and similar proteins; FBXO22, also called ...
153-183 3.61e-05

F-box domain found in F-box only protein 22 (FBXO22) and similar proteins; FBXO22, also called FBX22, or F-box protein FBX22p44, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. FBXO22 regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitin-mediated proteasomal 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: 438869  Cd Length: 48  Bit Score: 41.19  E-value: 3.61e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 17647819 153 FPELLEQIFEHLPVRDLGRAAQVCTAWRDAA 183
Cdd:cd22097   4 IAEIVERILSFLPAKALLRCARVCRLWRDCA 34
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
149-189 7.24e-05

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: 40.01  E-value: 7.24e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647819 149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVW 189
Cdd:cd22124   1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
435-533 8.20e-05

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: 44.65  E-value: 8.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647819 435 KISDQALTHIAQGL----YRLRSLSLNQCQITDHGMLKIAKALHE---LENLNIGQCSrITDKGLQTLAEDL---TNLKT 504
Cdd:cd00116 119 GLGDRGLRLLAKGLkdlpPALEKLVLGRNRLEGASCEALAKALRAnrdLKELNLANNG-IGDAGIRALAEGLkanCNLEV 197
                        90       100       110
                ....*....|....*....|....*....|...
gi 17647819 505 IDLYGCTqLSSKGI----DIIMKLPKLQKLNLG 533
Cdd:cd00116 198 LDLNNNG-LTDEGAsalaETLASLKSLEVLNLG 229
F-box_FBXL3 cd22178
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also ...
151-189 9.81e-05

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: 39.89  E-value: 9.81e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 17647819 151 NLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVW 189
Cdd:cd22178   5 NLLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
156-190 1.18e-04

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. 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: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 39.52  E-value: 1.18e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17647819 156 LLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22132   8 LLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWK 42
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
149-190 1.43e-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: 39.60  E-value: 1.43e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17647819 149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22147   2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWK 43
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
155-189 1.72e-04

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: 39.28  E-value: 1.72e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17647819 155 ELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVW 189
Cdd:cd22134  10 ELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLW 44
F-box_FBXO24 cd22098
F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called ...
148-189 2.26e-04

F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called FBX24, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It recognizes deacetylated nucleoside diphosphate kinase A (NDPK-A) to enhance its 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: 438870  Cd Length: 47  Bit Score: 38.84  E-value: 2.26e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17647819 148 HISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVW 189
Cdd:cd22098   1 SLLDLPPEILDRIISFLPVKDIVSLGQTCRYFHEVCNSEAVW 42
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
149-181 3.93e-04

F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called FBX42, or just one F-box and Kelch domain-containing protein (JFK), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It specifically recognizes p53/TP53, promoting its ubiquitination and degradation. FBXO42 is also involved in the ubiquitin-proteasome system that may play a role in the pathogenesis of Parkinson's disease (PD). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438882  Cd Length: 38  Bit Score: 38.09  E-value: 3.93e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 17647819 149 ISNLFPELLEQIFEHL-PVRDLGRAAQVCTAWRD 181
Cdd:cd22110   1 INDLPEEILEYILSYLsPYGDLKSAALVCKRWHR 34
F-box_FBXO17-like cd22169
F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and ...
149-190 4.34e-04

F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and similar proteins; This subfamily includes FBXO17 and FBXO27. FBXO17 is also called FBX17, F-box only protein 26 (FBX26/FBXO26), or FBG4, while FBXO27 is also called FBX27, or F-box/G-domain protein 5. FBXO17 and FBXO27 are the substrate-recognition components of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. They can recognize and bind denatured glycoproteins, which are modified with complex-type oligosaccharides. FBXO17 also recognizes sulfated glycans but does not bind high-mannose glycoproteins. 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: 438940  Cd Length: 48  Bit Score: 38.17  E-value: 4.34e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17647819 149 ISNLFPELLEQIFEHLPVRDL-GRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22169   1 LSLLPEELLLLVLSHVPARTLvTRCRLVCRDWRDLVDGPTLWK 43
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
150-189 8.34e-04

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: 37.01  E-value: 8.34e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVW 189
Cdd:cd22114   2 DSLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
148-181 9.03e-04

F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called FBX18, or F-box DNA helicase 1 (FBH1), is a 3'-5' DNA helicase and the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438867  Cd Length: 48  Bit Score: 37.25  E-value: 9.03e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17647819 148 HISNLFPELLEQIFEHLPVRDLGR-AAQVCTAWRD 181
Cdd:cd22095   1 HIQQLPEELLRNIFAFLPAEDLYQnISLVCRHWRD 35
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
155-199 1.65e-03

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. 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: 438889  Cd Length: 47  Bit Score: 36.45  E-value: 1.65e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17647819 155 ELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWKgveaKLHLK 199
Cdd:cd22117   7 ELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWK----ELNLQ 47
F-box_FBXO39 cd22108
F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called ...
154-190 1.84e-03

F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called FBX39, likely functions as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a cancer/testis antigen from colon cancer patients by serological analysis of recombinant cDNA expression libraries (SEREX). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438880  Cd Length: 44  Bit Score: 36.24  E-value: 1.84e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17647819 154 PEL-LEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22108   5 PDVcLRHVFRWLGDRDRSRAALVCKRWNQAMYSPALWR 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) ...
149-190 2.80e-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: 2.80e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17647819 149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22115   4 NKKLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
160-192 4.76e-03

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: 35.38  E-value: 4.76e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 17647819 160 IFEHLPVRDLGRAAQVCTAWRDAAYAKSVWKGV 192
Cdd:cd22109  14 VFSYLDTKSLLRCAEVCREWRDVSRHPALWQRV 46
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
155-190 5.28e-03

F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and similar proteins; DmSKP2 is a Drosophila F-box protein that regulates cell proliferation by targeting Dacapo (Dap) for ubiquitination and proteasome-mediated degradation. It plays a role in maintaining diploidy of mitotic cells during development. 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: 438920  Cd Length: 43  Bit Score: 35.04  E-value: 5.28e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 17647819 155 ELLEQIFEHLPVRDLGRAAQVCTAWRDAAYAKSVWK 190
Cdd:cd22149   7 EIILSIFKWLPKKTLARCARVCRRWKRLCFDESLWR 42
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
149-181 5.89e-03

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: 34.98  E-value: 5.89e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 17647819 149 ISNLFPELLEQIFEHLPVRDLGRAAQVCTAWRD 181
Cdd:cd22113   1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWND 33
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
150-179 5.92e-03

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: 34.57  E-value: 5.92e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAW 179
Cdd:cd22111   2 ARLPSRVLEVIFSYLDLPDLRNCSLVCKSW 31
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
473-496 6.77e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 6.77e-03
                           10        20
                   ....*....|....*....|....
gi 17647819    473 LHELENLNIGQCSRITDKGLQTLA 496
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
F-box_AtFBW2-like cd22158
F-box domain found in Arabidopsis thaliana F-box protein FBW2 (AtFBW2) and similar proteins; ...
150-179 7.19e-03

F-box domain found in Arabidopsis thaliana F-box protein FBW2 (AtFBW2) and similar proteins; AtFBW2, also called SKP1-interacting partner 18 (SKIP18), is an F-box protein that contains four tandem WD-40 repeats. It is a component of SCF (SPK1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with CUL1, CUL2 and SPK1B/ASK2. 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: 438929  Cd Length: 36  Bit Score: 34.36  E-value: 7.19e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 17647819 150 SNLFPELLEQIFEHLPVRDLGRAAQVCTAW 179
Cdd:cd22158   2 DCLPPDLLELIFSHLPLHDILICRSVCKFW 31
 
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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