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Conserved domains on  [gi|1958767707|ref|XP_038962809|]
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F-box and leucine-rich repeat protein 13 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 525-733 4.96e-20

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: 89.69  E-value: 4.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 525 LTDSSLKSLSVL--KQLTVLNLTNCVRIgDIGLRQFFdgpASVKLRELNLANCSLLGDTSVIRLSERCPNLHYLNLRNCE 602
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 603 HLTDLAIEYIASMLSLIsidlsgTLISneglaiLSRHRKlrevslseCVNITDFGIRAFCKTSLALEHLDVSYCaQLTDD 682
Cdd:cd09293    90 NITDSGIVALATNCPKL------QTIN------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTDK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958767707 683 IIKTIAIFC-TRITSLHIAGCPKITDGGMEIL--SARCHYLHILDISGCVQLTD 733
Cdd:cd09293   149 GVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITD 202
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 9-50 1.36e-16

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


:

Pssm-ID: 438546  Cd Length: 43  Bit Score: 73.74  E-value: 1.36e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707   9 PRLRNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22977     2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 308-477 6.65e-12

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


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 65.81  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 308 NVLRLNFRGCVLRAKTLKSVSHCKNLQELNVSDCPSFTDESMRHISEGCPGVLYLNLSN-TTITNRTMRLLPRYFHNLQN 386
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 387 LSLAY---CRKFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRNIANSC-TGIMHLTINDMPTLTDNCVKVLVEK-- 460
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170
                  ....*....|....*..
gi 1958767707 461 CPRISSVVFIGSPHISD 477
Cdd:cd09293   186 FPNLSVLEFRGCPLITD 202
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 242-283 3.42e-11

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.


The actual alignment was detected with superfamily member cd22124:

Pssm-ID: 459239  Cd Length: 42  Bit Score: 58.50  E-value: 3.42e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
DUF4659 super family cl37893
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 115-220 1.89e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


The actual alignment was detected with superfamily member pfam15558:

Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.56  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 115 WKEIaipHANQEAIMAEKMDKAIAHDNFR--CQKHIFNRWFSYTVKRRERLIATLLRL-------RHLFYTQKQ-RIILA 184
Cdd:pfam15558  96 WREQ---AEDQENQRQEKLERARQEAEQRkqCQEQRLKEKEEELQALREQNSLQLQERleeachkRQLKEREEQkKVQEN 172

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958767707 185 KWKEKARHKSKKREDDLITKHELQLKkwkfKLSLEK 220
Cdd:pfam15558 173 NLSELLNHQARKVLVDCQAKAEELLR----RLSLEQ 204
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 525-733 4.96e-20

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: 89.69  E-value: 4.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 525 LTDSSLKSLSVL--KQLTVLNLTNCVRIgDIGLRQFFdgpASVKLRELNLANCSLLGDTSVIRLSERCPNLHYLNLRNCE 602
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 603 HLTDLAIEYIASMLSLIsidlsgTLISneglaiLSRHRKlrevslseCVNITDFGIRAFCKTSLALEHLDVSYCaQLTDD 682
Cdd:cd09293    90 NITDSGIVALATNCPKL------QTIN------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTDK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958767707 683 IIKTIAIFC-TRITSLHIAGCPKITDGGMEIL--SARCHYLHILDISGCVQLTD 733
Cdd:cd09293   149 GVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITD 202
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 9-50 1.36e-16

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438546  Cd Length: 43  Bit Score: 73.74  E-value: 1.36e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707   9 PRLRNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22977     2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 308-477 6.65e-12

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 65.81  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 308 NVLRLNFRGCVLRAKTLKSVSHCKNLQELNVSDCPSFTDESMRHISEGCPGVLYLNLSN-TTITNRTMRLLPRYFHNLQN 386
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 387 LSLAY---CRKFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRNIANSC-TGIMHLTINDMPTLTDNCVKVLVEK-- 460
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170
                  ....*....|....*..
gi 1958767707 461 CPRISSVVFIGSPHISD 477
Cdd:cd09293   186 FPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 242-283 3.42e-11

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: 58.50  E-value: 3.42e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
518-740 4.21e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 62.64  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 518 YMVDCKGLTDSSLKSLSVLKQLTVLNLTNCvRIGDIG--LRQFfdgpasVKLRELNLANCSLlgdTSVIRLSERCPNLHY 595
Cdd:COG4886    94 DLTNLTELDLSGNEELSNLTNLESLDLSGN-QLTDLPeeLANL------TNLKELDLSNNQL---TDLPEPLGNLTNLKS 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 596 LNLRNCEhLTDLAIEyIASMLSLISIDLSGTLISNEGLAiLSRHRKLREVSLSECvNITDFGirafckTSLA----LEHL 671
Cdd:COG4886   164 LDLSNNQ-LTDLPEE-LGNLTNLKELDLSNNQITDLPEP-LGNLTNLEELDLSGN-QLTDLP------EPLAnltnLETL 233

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958767707 672 DVSYCaQLTDdiIKTIAiFCTRITSLHIAGCpKITDGGMeilSARCHYLHILDISGCvQLTDQILQDLQ 740
Cdd:COG4886   234 DLSNN-QLTD--LPELG-NLTNLEELDLSNN-QLTDLPP---LANLTNLKTLDLSNN-QLTDLKLKELE 293
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 242-286 1.92e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 53.64  E-value: 1.92e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWNSID 286
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
307-636 7.98e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 42.61  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 307 LNVLRLNFRGCVLRAKTLKSVSHCKNLQELNVSDCPSFTDesmrhisegCPGVLYLNLSNTTITNrtmrlLPRYFHNLQN 386
Cdd:COG4886    72 LLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPEELANLTN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 387 lslaycrkftdkgLQYLNLGN-----------GCHKLIYLDLSGCtQISvqgfrNIANSCTGIMHLTINDmptLTDNcvk 455
Cdd:COG4886   138 -------------LKELDLSNnqltdlpeplgNLTNLKSLDLSNN-QLT-----DLPEELGNLTNLKELD---LSNN--- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 456 vlvekcpRISSVvfigSPHISDCAfkalsacDLKKIRFEGNKrITDacfksvdrnypgIShiymvdckgltdsslKSLSV 535
Cdd:COG4886   193 -------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTD------------LP---------------EPLAN 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 536 LKQLTVLNLTNCvRIGDI-GLRQFfdgpasVKLRELNLANCSLlgdtSVIRLSERCPNLHYLNLRNCeHLTDLAIEYIAS 614
Cdd:COG4886   227 LTNLETLDLSNN-QLTDLpELGNL------TNLEELDLSNNQL----TDLPPLANLTNLKTLDLSNN-QLTDLKLKELEL 294

                         330       340
                  ....*....|....*....|..
gi 1958767707 615 MLSLISIDLSGTLISNEGLAIL 636
Cdd:COG4886   295 LLGLNSLLLLLLLLNLLELLIL 316
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
330-355 8.82e-04

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 37.39  E-value: 8.82e-04
                           10        20
                   ....*....|....*....|....*.
gi 1958767707  330 CKNLQELNVSDCPSFTDESMRHISEG 355
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 566-607 1.31e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 37.22  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707 566 KLRELNLANCSLlgdtSVIRLSERCPNLHYLNLRNCEHLTDL 607
Cdd:pfam12799   2 NLEVLDLSNNQI----TDIPPLAKLPNLETLDLSGNNKITDL 39
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
590-614 1.36e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 36.62  E-value: 1.36e-03
                           10        20
                   ....*....|....*....|....*
gi 1958767707  590 CPNLHYLNLRNCEHLTDLAIEYIAS 614
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25
FBOX smart00256
A Receptor for Ubiquitination Targets;
245-283 1.88e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.65  E-value: 1.88e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958767707  245 LPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 115-220 1.89e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.56  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 115 WKEIaipHANQEAIMAEKMDKAIAHDNFR--CQKHIFNRWFSYTVKRRERLIATLLRL-------RHLFYTQKQ-RIILA 184
Cdd:pfam15558  96 WREQ---AEDQENQRQEKLERARQEAEQRkqCQEQRLKEKEEELQALREQNSLQLQERleeachkRQLKEREEQkKVQEN 172

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958767707 185 KWKEKARHKSKKREDDLITKHELQLKkwkfKLSLEK 220
Cdd:pfam15558 173 NLSELLNHQARKVLVDCQAKAEELLR----RLSLEQ 204
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 525-733 4.96e-20

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: 89.69  E-value: 4.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 525 LTDSSLKSLSVL--KQLTVLNLTNCVRIgDIGLRQFFdgpASVKLRELNLANCSLLGDTSVIRLSERCPNLHYLNLRNCE 602
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 603 HLTDLAIEYIASMLSLIsidlsgTLISneglaiLSRHRKlrevslseCVNITDFGIRAFCKTSLALEHLDVSYCaQLTDD 682
Cdd:cd09293    90 NITDSGIVALATNCPKL------QTIN------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTDK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958767707 683 IIKTIAIFC-TRITSLHIAGCPKITDGGMEIL--SARCHYLHILDISGCVQLTD 733
Cdd:cd09293   149 GVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITD 202
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 9-50 1.36e-16

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438546  Cd Length: 43  Bit Score: 73.74  E-value: 1.36e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707   9 PRLRNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22977     2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 308-477 6.65e-12

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 65.81  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 308 NVLRLNFRGCVLRAKTLKSVSHCKNLQELNVSDCPSFTDESMRHISEGCPGVLYLNLSN-TTITNRTMRLLPRYFHNLQN 386
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 387 LSLAY---CRKFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRNIANSC-TGIMHLTINDMPTLTDNCVKVLVEK-- 460
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170
                  ....*....|....*..
gi 1958767707 461 CPRISSVVFIGSPHISD 477
Cdd:cd09293   186 FPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 242-283 3.42e-11

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: 58.50  E-value: 3.42e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 475-607 4.08e-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: 63.50  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 475 ISDCAFKALSAC-DLKKIRFEGNKRITDACFKSVDRNYPGISHIYMVDCKGLTDSSLKSLSV-LKQLTVLNL---TNCVR 549
Cdd:cd09293    40 ISDPPLDQLSNCnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQTINLgrhRNGHL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 550 IGDIGLRQF-----------FDG----PASV---------KLRELNLANCSLLGDTSV--IRLSERCPNLHYLNLRNCEH 603
Cdd:cd09293   120 ITDVSLSALgknctflqtvgFAGcdvtDKGVwelasgcskSLERLSLNNCRNLTDQSIpaILASNYFPNLSVLEFRGCPL 199


                  ....
gi 1958767707 604 LTDL 607
Cdd:cd09293   200 ITDF 203
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
518-740 4.21e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 62.64  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 518 YMVDCKGLTDSSLKSLSVLKQLTVLNLTNCvRIGDIG--LRQFfdgpasVKLRELNLANCSLlgdTSVIRLSERCPNLHY 595
Cdd:COG4886    94 DLTNLTELDLSGNEELSNLTNLESLDLSGN-QLTDLPeeLANL------TNLKELDLSNNQL---TDLPEPLGNLTNLKS 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 596 LNLRNCEhLTDLAIEyIASMLSLISIDLSGTLISNEGLAiLSRHRKLREVSLSECvNITDFGirafckTSLA----LEHL 671
Cdd:COG4886   164 LDLSNNQ-LTDLPEE-LGNLTNLKELDLSNNQITDLPEP-LGNLTNLEELDLSGN-QLTDLP------EPLAnltnLETL 233

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958767707 672 DVSYCaQLTDdiIKTIAiFCTRITSLHIAGCpKITDGGMeilSARCHYLHILDISGCvQLTDQILQDLQ 740
Cdd:COG4886   234 DLSNN-QLTD--LPELG-NLTNLEELDLSNN-QLTDLPP---LANLTNLKTLDLSNN-QLTDLKLKELE 293
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 242-286 1.92e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 53.64  E-value: 1.92e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWNSID 286
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 667-761 2.23e-09

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 58.49  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 667 ALEHLDVSYCAQLtdDIIKTIAIFCTRITSLHIAGCPKITDGGMEILSARCHYLHILDISGCVQLTDQILQDLQIGCKQL 746
Cdd:cd09293    29 GLEWLELYMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106

                          90
                  ....*....|....*...
gi 1958767707 747 RIL---KMQFCKSISSAA 761
Cdd:cd09293   107 QTInlgRHRNGHLITDVS 124
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 562-750 8.63e-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: 54.67  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 562 PASVKLRELNLANCSLLGDTS--VIRLSeRCPNLHYLNLRNCEhLTDLAIEYIASML-----SLISIDLSGTLISNEGLA 634
Cdd:cd00116    78 TKGCGLQELDLSDNALGPDGCgvLESLL-RSSSLQELKLNNNG-LGDRGLRLLAKGLkdlppALEKLVLGRNRLEGASCE 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 635 ----ILSRHRKLREVSLSECvNITDFGIRAFC---KTSLALEHLDVSYCaQLTDDIIKTIA-IFCT--RITSLHIAGCPk 704
Cdd:cd00116   156 alakALRANRDLKELNLANN-GIGDAGIRALAeglKANCNLEVLDLNNN-GLTDEGASALAeTLASlkSLEVLNLGDNN- 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958767707 705 ITDGGM----EILSARCHYLHILDISgCVQLTDQILQDLQIGCKQLRILK 750
Cdd:cd00116   233 LTDAGAaalaSALLSPNISLLTLSLS-CNDITDDGAKDLAEVLAEKESLL 281
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 242-282 3.86e-07

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: 46.95  E-value: 3.86e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22118     1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 12-50 9.44e-07

dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55)-like family; The TEX55-like family includes TEX55, F-box/LRR-repeat protein 13 (FBXL13), adenylate kinase isoenzymes AK5 and AK8, as well as uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), and protein VEST-1. TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. AK5 and AK8 act as nucleoside monophosphate (NMP) kinases that catalyze the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Members of this family contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438530  Cd Length: 43  Bit Score: 45.87  E-value: 9.44e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958767707  12 RNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22961     5 EEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQI 43
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
 240-285 1.93e-06

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: 45.45  E-value: 1.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958767707 240 FDISvLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWNSI 285
Cdd:cd22134     3 FDIQ-LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 12-50 6.73e-06

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438547  Cd Length: 44  Bit Score: 43.68  E-value: 6.73e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958767707  12 RNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22978     5 KDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKI 43
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 243-288 1.57e-05

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438876  Cd Length: 48  Bit Score: 42.63  E-value: 1.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958767707 243 SVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWNSIDFS 288
Cdd:cd22104     2 ANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRLH 47
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 242-282 3.23e-05

F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) and similar proteins; DdgacFF, also called GTPase activating factor for raC protein FF, is a Rho GTPase-activating protein involved in the signal transduction 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: 438919  Cd Length: 44  Bit Score: 41.88  E-value: 3.23e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22148     2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELW 42
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 575-734 6.37e-05

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 46.32  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 575 CSLLGDTSVIRLSE---RCPNLHYLNLRNcEHLTDLAIEYIASML----SLISIDLSGTLISNEGLAILSRH----RKLR 643
Cdd:COG5238   189 CNQIGDEGIEELAEaltQNTTVTTLWLKR-NPIGDEGAEILAEALkgnkSLTTLDLSNNQIGDEGVIALAEAlknnTTVE 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 644 EVSLSeCVNITDFGIRAFCK---TSLALEHLDVSYcAQLTDD----IIKTIAIFCTrITSLHIAGCpKITDGGMEILSA- 715
Cdd:COG5238   268 TLYLS-GNQIGAEGAIALAKalqGNTTLTSLDLSV-NRIGDEgaiaLAEGLQGNKT-LHTLNLAYN-GIGAQGAIALAKa 343

                         170       180
                  ....*....|....*....|.
gi 1958767707 716 -RCHY-LHILDISGCvQLTDQ 734
Cdd:COG5238   344 lQENTtLHSLDLSDN-QIGDE 363
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
 245-285 8.03e-05

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, 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 Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. 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: 438892  Cd Length: 44  Bit Score: 40.45  E-value: 8.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 245 LPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWNSI 285
Cdd:cd22120     4 LPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 245-282 2.83e-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: 39.13  E-value: 2.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958767707 245 LPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22132     4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 245-270 2.94e-04

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). 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: 438856  Cd Length: 49  Bit Score: 39.16  E-value: 2.94e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958767707 245 LPDQAVVQIFVYLTFKDLVSCSQVNR 270
Cdd:cd22084     4 LPSDPLLNILSFLDYRDLISCSQVCR 29
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 531-648 3.85e-04

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: 43.63  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 531 KSLSVLKQLTVLNLtNCVRIGDIGLRQFFDGPASVK-LRELNLANCSLlGDTSVIRLSE---RCPNLHYLNLRNCE---H 603
Cdd:COG5238   286 KALQGNTTLTSLDL-SVNRIGDEGAIALAEGLQGNKtLHTLNLAYNGI-GAQGAIALAKalqENTTLHSLDLSDNQigdE 363

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958767707 604 LTDLAIEYIASMLSLISIDLSGTLISNEG---LAILSRHRKLREVSLS 648
Cdd:COG5238   364 GAIALAKYLEGNTTLRELNLGKNNIGKQGaeaLIDALQTNRLHTLILD 411
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 243-277 3.98e-04

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: 38.19  E-value: 3.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958767707 243 SVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQ 277
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 242-282 4.44e-04

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 38.29  E-value: 4.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLW 41
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
 253-282 6.10e-04

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: 38.08  E-value: 6.10e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958767707 253 IFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22109    14 VFSYLDTKSLLRCAEVCREWRDVSRHPALW 43
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
307-636 7.98e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 42.61  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 307 LNVLRLNFRGCVLRAKTLKSVSHCKNLQELNVSDCPSFTDesmrhisegCPGVLYLNLSNTTITNrtmrlLPRYFHNLQN 386
Cdd:COG4886    72 LLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPEELANLTN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 387 lslaycrkftdkgLQYLNLGN-----------GCHKLIYLDLSGCtQISvqgfrNIANSCTGIMHLTINDmptLTDNcvk 455
Cdd:COG4886   138 -------------LKELDLSNnqltdlpeplgNLTNLKSLDLSNN-QLT-----DLPEELGNLTNLKELD---LSNN--- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 456 vlvekcpRISSVvfigSPHISDCAfkalsacDLKKIRFEGNKrITDacfksvdrnypgIShiymvdckgltdsslKSLSV 535
Cdd:COG4886   193 -------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTD------------LP---------------EPLAN 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 536 LKQLTVLNLTNCvRIGDI-GLRQFfdgpasVKLRELNLANCSLlgdtSVIRLSERCPNLHYLNLRNCeHLTDLAIEYIAS 614
Cdd:COG4886   227 LTNLETLDLSNN-QLTDLpELGNL------TNLEELDLSNNQL----TDLPPLANLTNLKTLDLSNN-QLTDLKLKELEL 294

                         330       340
                  ....*....|....*....|..
gi 1958767707 615 MLSLISIDLSGTLISNEGLAIL 636
Cdd:COG4886   295 LLGLNSLLLLLLLLNLLELLIL 316
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
330-355 8.82e-04

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 37.39  E-value: 8.82e-04
                           10        20
                   ....*....|....*....|....*.
gi 1958767707  330 CKNLQELNVSDCPSFTDESMRHISEG 355
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 242-282 1.10e-03

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: 37.33  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22123     1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 566-607 1.31e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 37.22  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707 566 KLRELNLANCSLlgdtSVIRLSERCPNLHYLNLRNCEHLTDL 607
Cdd:pfam12799   2 NLEVLDLSNNQI----TDIPPLAKLPNLETLDLSGNNKITDL 39
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
590-614 1.36e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 36.62  E-value: 1.36e-03
                           10        20
                   ....*....|....*....|....*
gi 1958767707  590 CPNLHYLNLRNCEHLTDLAIEYIAS 614
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
 242-282 1.49e-03

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: 37.29  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22147     2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELW 42
FBOX smart00256
A Receptor for Ubiquitination Targets;
245-283 1.88e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.65  E-value: 1.88e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958767707  245 LPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 115-220 1.89e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.56  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 115 WKEIaipHANQEAIMAEKMDKAIAHDNFR--CQKHIFNRWFSYTVKRRERLIATLLRL-------RHLFYTQKQ-RIILA 184
Cdd:pfam15558  96 WREQ---AEDQENQRQEKLERARQEAEQRkqCQEQRLKEKEEELQALREQNSLQLQERleeachkRQLKEREEQkKVQEN 172

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958767707 185 KWKEKARHKSKKREDDLITKHELQLKkwkfKLSLEK 220
Cdd:pfam15558 173 NLSELLNHQARKVLVDCQAKAEELLR----RLSLEQ 204
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 245-272 1.94e-03

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: 36.57  E-value: 1.94e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958767707 245 LPDQAVVQIFVYLTFKDLVSCSQVNRSW 272
Cdd:cd22121     3 LPEEILVHIFRHLSLRDRYAAAQVCKHW 30
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
 245-272 2.77e-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: 36.11  E-value: 2.77e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958767707 245 LPDQAVVQIFVYLTFKDLVSCSQVNRSW 272
Cdd:cd22111     4 LPSRVLEVIFSYLDLPDLRNCSLVCKSW 31
Sfi1 pfam08457
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 134-214 3.51e-03

Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.


Pssm-ID: 430007 [Multi-domain]  Cd Length: 570  Bit Score: 40.74  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 134 DKAIAHDNFRCQKHIFNRWFSYTVKRRERLIATLlrlrhLFYTQ--KQRiILAKWKEKARHKSK--KREDD----LITKH 205
Cdd:pfam08457 324 EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAAN-----EFYAPrlLQE-ALDAWRERHQHVQKleKWARDarfyFLATR 397


                  ....*....
gi 1958767707 206 elQLKKWKF 214
Cdd:pfam08457 398 --TLKKWRA 404
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
 243-285 3.68e-03

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: 35.76  E-value: 3.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958767707 243 SVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWNSI 285
Cdd:cd22151     1 RKLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENA 43
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 567-644 4.64e-03

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 40.50  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767707 567 LRELNLANCSLLGdTSVIRLSERCPNLHYLNLRNCeHLTDLAIEYIASMLSL---ISIDLS----GTLISNEGLAILSRH 639
Cdd:pfam19729  12 IQQLSLSGCYWLS-GSTVDQVTRCRNLVKLDLSGC-RLTSLRLSKLLSSLQHlrsLAIDVNpgfdASQLSSECKATLSRV 89


                  ....*
gi 1958767707 640 RKLRE 644
Cdd:pfam19729  90 RELKQ 94
F-box_ScCDC4-like cd22141
F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and ...
 242-282 5.41e-03

F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and similar proteins; ScCDC4 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 is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. 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: 438913  Cd Length: 47  Bit Score: 35.62  E-value: 5.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22141     1 IGNLPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALW 41
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
 242-282 7.45e-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: 35.09  E-value: 7.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958767707 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22115     4 NKKLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNW 44
F-box_AtADLO1-like cd22155
F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; ...
 241-282 8.93e-03

F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; AtADLO1, also called F-box only protein 5 (FBX5), promotes lateral root initiation and development, independently of auxin (IAA) and abscisic acid (ABA). 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: 438926  Cd Length: 42  Bit Score: 34.85  E-value: 8.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767707 241 DISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22155     1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42
 
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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