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Conserved domains on  [gi|294660155|ref|XP_462606|]
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DEHA2G24486p [Debaryomyces hansenii CBS767]

Protein Classification

F-box protein( domain architecture ID 15978888)

F-box protein is the substrate-recognition component of a SCF(Skp1-cullin-F-box) E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins

CATH:  1.20.1280.50
Gene Ontology:  GO:0019005|GO:0005515
PubMed:  10581972|31898225|11178263
SCOP:  4001927

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 ...
 198-373 1.23e-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: 91.23  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 198 CPKLERLTLVNCTKLTYSPvtSVLKNCEKLQSIDLTGVTGIHDDIILALANNCPRLQGLYAPGCGKVSEDAILKLLKSCP 277
Cdd:cd09293   27 HSGLEWLELYMCPISDPPL--DQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 278 MLKRVKF---NGSANITDRSIEAMHENCKSLVEIDLHNCsNVTDKYL-KLIFLNLSQLREFRISNAAGVTDRLFELLPSE 353
Cdd:cd09293  105 KLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAILAS 183

                        170       180
                 ....*....|....*....|
gi 294660155 354 YYLEKLRIVDITGCNAITDR 373
Cdd:cd09293  184 NYFPNLSVLEFRGCPLITDF 203
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 323-521 6.27e-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: 86.23  E-value: 6.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 323 LIFLNLSQLREFRIsnaagvtDRLFELLPSEyyLEKLrivDITGCNAITDRLieKLVMCAPRLRNVVLSKCMQITDASLR 402
Cdd:cd09293    6 FILHKLGQITQSNI-------SQLLRILHSG--LEWL---ELYMCPISDPPL--DQLSNCNKLKKLILPGSKLIDDEGLI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 403 ALSQLGRSLHYIHLGHCGLITDFGVASLVRSCHRIQYIDLAC---CSQLTDWTLVELA-NLPKLRRIGLVKCSlISDSGI 478
Cdd:cd09293   72 ALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGkNCTFLQTVGFAGCD-VTDKGV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 294660155 479 LELVRRRGEQdcLERVHLSYCTNLTIGPI-------------YLLLKNCPKLTHLS 521
Cdd:cd09293  151 WELASGCSKS--LERLSLNNCRNLTDQSIpailasnyfpnlsVLEFRGCPLITDFS 204
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 103-145 5.11e-09

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


:

Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 52.49  E-value: 5.11e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 294660155  103 LLNLPTEILLQIFHHLDRKELYSLLTVCHEFADLII-EILWFRP 145
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASdDSLWRRL 44
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 198-373 1.23e-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: 91.23  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 198 CPKLERLTLVNCTKLTYSPvtSVLKNCEKLQSIDLTGVTGIHDDIILALANNCPRLQGLYAPGCGKVSEDAILKLLKSCP 277
Cdd:cd09293   27 HSGLEWLELYMCPISDPPL--DQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 278 MLKRVKF---NGSANITDRSIEAMHENCKSLVEIDLHNCsNVTDKYL-KLIFLNLSQLREFRISNAAGVTDRLFELLPSE 353
Cdd:cd09293  105 KLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAILAS 183

                        170       180
                 ....*....|....*....|
gi 294660155 354 YYLEKLRIVDITGCNAITDR 373
Cdd:cd09293  184 NYFPNLSVLEFRGCPLITDF 203
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 323-521 6.27e-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: 6.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 323 LIFLNLSQLREFRIsnaagvtDRLFELLPSEyyLEKLrivDITGCNAITDRLieKLVMCAPRLRNVVLSKCMQITDASLR 402
Cdd:cd09293    6 FILHKLGQITQSNI-------SQLLRILHSG--LEWL---ELYMCPISDPPL--DQLSNCNKLKKLILPGSKLIDDEGLI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 403 ALSQLGRSLHYIHLGHCGLITDFGVASLVRSCHRIQYIDLAC---CSQLTDWTLVELA-NLPKLRRIGLVKCSlISDSGI 478
Cdd:cd09293   72 ALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGkNCTFLQTVGFAGCD-VTDKGV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 294660155 479 LELVRRRGEQdcLERVHLSYCTNLTIGPI-------------YLLLKNCPKLTHLS 521
Cdd:cd09293  151 WELASGCSKS--LERLSLNNCRNLTDQSIpailasnyfpnlsVLEFRGCPLITDFS 204
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 103-145 5.11e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 52.49  E-value: 5.11e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 294660155  103 LLNLPTEILLQIFHHLDRKELYSLLTVCHEFADLII-EILWFRP 145
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASdDSLWRRL 44
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 104-137 1.25e-05

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 42.43  E-value: 1.25e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 294660155 104 LNLPTEILLQIFHHLDRKELYSLLTVCHEFADLI 137
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
300-579 2.89e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 300 ENCKSLVEIDLHNCsNVTDkyLKLIFLNLSQLREFRISNaagvtDRLFELLPSEYYLEKLRIVDITGcNAITD--RLIEK 377
Cdd:COG4886  110 SNLTNLESLDLSGN-QLTD--LPEELANLTNLKELDLSN-----NQLTDLPEPLGNLTNLKSLDLSN-NQLTDlpEELGN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 378 LvmcaPRLRNVVLSKCmQITDASLrALSQLgRSLHYIHLGHCGlITDFGVAslVRSCHRIQYIDLACCsQLTDwtLVELA 457
Cdd:COG4886  181 L----TNLKELDLSNN-QITDLPE-PLGNL-TNLEELDLSGNQ-LTDLPEP--LANLTNLETLDLSNN-QLTD--LPELG 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 458 NLPKLRRIGLVKCSLISDSGILELVRrrgeqdcLERVHLSYC--TNLTIGPIYLLLK-NCPKLTHLSLTGISAFLRREIT 534
Cdd:COG4886  248 NLTNLEELDLSNNQLTDLPPLANLTN-------LKTLDLSNNqlTDLKLKELELLLGlNSLLLLLLLLNLLELLILLLLL 320

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 294660155 535 QYCRDPPPDFNEQQKNSFCVFSGNGVSQLRNHLNQIMEDRSYLID 579
Cdd:COG4886  321 TTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
84-378 6.93e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.53  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155  84 SSTSNHRNEIQKLNYKNSLLLNLPTEILLQIFHHLDRKELYSLLTVCHEFADLIIEILWFRPNMQNDDSFKKIKTIMEIP 163
Cdd:COG4886    7 SLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 164 KGGTHWDYRSFIKRLNLSFMTKLVD-DDLLKLFVGCPKLERL--TLVNCTKLTY--------SPVTSVLKNCEKLQSIDL 232
Cdd:COG4886   87 LGLTDLGDLTNLTELDLSGNEELSNlTNLESLDLSGNQLTDLpeELANLTNLKEldlsnnqlTDLPEPLGNLTNLKSLDL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 233 --TGVTGIHDDIilalaNNCPRLQGLYAPGCgKVSEdaILKLLKSCPMLKRVKFNGSaNITDrsIEAMHENCKSLVEIDL 310
Cdd:COG4886  167 snNQLTDLPEEL-----GNLTNLKELDLSNN-QITD--LPEPLGNLTNLEELDLSGN-QLTD--LPEPLANLTNLETLDL 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294660155 311 HNCsNVTDkylkLIFL-NLSQLREFRISNaAGVTDrlfelLPSEYYLEKLRIVDITGcNAITDRLIEKL 378
Cdd:COG4886  236 SNN-QLTD----LPELgNLTNLEELDLSN-NQLTD-----LPPLANLTNLKTLDLSN-NQLTDLKLKEL 292
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 198-373 1.23e-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: 91.23  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 198 CPKLERLTLVNCTKLTYSPvtSVLKNCEKLQSIDLTGVTGIHDDIILALANNCPRLQGLYAPGCGKVSEDAILKLLKSCP 277
Cdd:cd09293   27 HSGLEWLELYMCPISDPPL--DQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 278 MLKRVKF---NGSANITDRSIEAMHENCKSLVEIDLHNCsNVTDKYL-KLIFLNLSQLREFRISNAAGVTDRLFELLPSE 353
Cdd:cd09293  105 KLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAILAS 183

                        170       180
                 ....*....|....*....|
gi 294660155 354 YYLEKLRIVDITGCNAITDR 373
Cdd:cd09293  184 NYFPNLSVLEFRGCPLITDF 203
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 323-521 6.27e-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: 6.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 323 LIFLNLSQLREFRIsnaagvtDRLFELLPSEyyLEKLrivDITGCNAITDRLieKLVMCAPRLRNVVLSKCMQITDASLR 402
Cdd:cd09293    6 FILHKLGQITQSNI-------SQLLRILHSG--LEWL---ELYMCPISDPPL--DQLSNCNKLKKLILPGSKLIDDEGLI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 403 ALSQLGRSLHYIHLGHCGLITDFGVASLVRSCHRIQYIDLAC---CSQLTDWTLVELA-NLPKLRRIGLVKCSlISDSGI 478
Cdd:cd09293   72 ALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGkNCTFLQTVGFAGCD-VTDKGV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 294660155 479 LELVRRRGEQdcLERVHLSYCTNLTIGPI-------------YLLLKNCPKLTHLS 521
Cdd:cd09293  151 WELASGCSKS--LERLSLNNCRNLTDQSIpailasnyfpnlsVLEFRGCPLITDFS 204
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 175-367 2.18e-17

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: 81.99  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 175 IKRLNLsFMTKLVDDDLLKLFVgCPKLERLTLVNCTKLTYSPVTSVLKNCEKLQSIDLTGVTGIHDDIILALANNCPRLQ 254
Cdd:cd09293   30 LEWLEL-YMCPISDPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 255 GL---YAPGCGKVSEDAILKLLKSCPMLKRVKFNGSaNITDRSIEAMHENC-KSLVEIDLHNCSNVTDKYLKLIF--LNL 328
Cdd:cd09293  108 TInlgRHRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILasNYF 186

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 294660155 329 SQLREFRISNAAGVTDRLFELLPSEYYLEKLRIVDITGC 367
Cdd:cd09293  187 PNLSVLEFRGCPLITDFSRIILFKLWQPRLNKPILVEWC 225
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 103-145 5.11e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 52.49  E-value: 5.11e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 294660155  103 LLNLPTEILLQIFHHLDRKELYSLLTVCHEFADLII-EILWFRP 145
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASdDSLWRRL 44
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 325-499 5.58e-06

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: 48.89  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 325 FLNLSQLREFRISNAAGVTD--RLFELLPSEYYLEKLRIVDITGCNAITDRLIEKLVMCAPRLRNVVLSKCmQITDASLR 402
Cdd:cd00116   77 LTKGCGLQELDLSDNALGPDgcGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRN-RLEGASCE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 403 ALS---QLGRSLHYIHLGHCGlITDFGVASLVR----SCHrIQYIDLACCsQLTDWTLVELA----NLPKLRRIGLVKCs 471
Cdd:cd00116  156 ALAkalRANRDLKELNLANNG-IGDAGIRALAEglkaNCN-LEVLDLNNN-GLTDEGASALAetlaSLKSLEVLNLGDN- 231

                        170       180
                 ....*....|....*....|....*....
gi 294660155 472 LISDSGILELVRR-RGEQDCLERVHLSYC 499
Cdd:cd00116  232 NLTDAGAAALASAlLSPNISLLTLSLSCN 260
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 104-137 1.25e-05

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 42.43  E-value: 1.25e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 294660155 104 LNLPTEILLQIFHHLDRKELYSLLTVCHEFADLI 137
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34
F-box_ScMDM30-like cd22143
F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology ...
 103-145 1.22e-04

F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology protein 30 (ScMDM30) and similar proteins; ScMDM30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. It 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. ScMDM30 recognizes FZO1 and regulates the amount of FZO1. It acts as a regulatory factor for the mitochondrial fusion machinery and is required for mitochondrial DNA maintenance. 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: 438915  Cd Length: 44  Bit Score: 39.90  E-value: 1.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 294660155 103 LLNLPTEILLQIFHHLDRKELYSLLTVCHEFADLIIEILWFRP 145
Cdd:cd22143    2 FDSLPDEILSIIFSHLPQSDLYNLLFVNKHFYSLALPELWRSI 44
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 103-137 2.15e-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: 39.06  E-value: 2.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 294660155  103 LLNLPTEILLQIFHHLDRKELYSLLTVCHEFADLI 137
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLV 35
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 105-144 1.40e-03

F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called FBX15, has a novel dual molecular function by controlling transcriptional repression and being part of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligases, which is essential for stress response, gliotoxin production and virulence in the opportunistic human pathogen Aspergillus fumigatus. 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: 438865  Cd Length: 46  Bit Score: 36.85  E-value: 1.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 294660155 105 NLPTEILLQIFHHLDRKELYSLLTVCHEFADLI-IEILWFR 144
Cdd:cd22093    3 RLPSEILLKILSYLDASSLLCISCVNKLFYQLAnDNALWRK 43
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 103-136 1.48e-03

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: 37.24  E-value: 1.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 294660155 103 LLNLPTEILLQIFHHLDRKELYSLLTVCHEFADL 136
Cdd:cd22084    1 LDDLPSDPLLNILSFLDYRDLISCSQVCRRLNQL 34
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
300-579 2.89e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 300 ENCKSLVEIDLHNCsNVTDkyLKLIFLNLSQLREFRISNaagvtDRLFELLPSEYYLEKLRIVDITGcNAITD--RLIEK 377
Cdd:COG4886  110 SNLTNLESLDLSGN-QLTD--LPEELANLTNLKELDLSN-----NQLTDLPEPLGNLTNLKSLDLSN-NQLTDlpEELGN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 378 LvmcaPRLRNVVLSKCmQITDASLrALSQLgRSLHYIHLGHCGlITDFGVAslVRSCHRIQYIDLACCsQLTDwtLVELA 457
Cdd:COG4886  181 L----TNLKELDLSNN-QITDLPE-PLGNL-TNLEELDLSGNQ-LTDLPEP--LANLTNLETLDLSNN-QLTD--LPELG 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 458 NLPKLRRIGLVKCSLISDSGILELVRrrgeqdcLERVHLSYC--TNLTIGPIYLLLK-NCPKLTHLSLTGISAFLRREIT 534
Cdd:COG4886  248 NLTNLEELDLSNNQLTDLPPLANLTN-------LKTLDLSNNqlTDLKLKELELLLGlNSLLLLLLLLNLLELLILLLLL 320

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 294660155 535 QYCRDPPPDFNEQQKNSFCVFSGNGVSQLRNHLNQIMEDRSYLID 579
Cdd:COG4886  321 TTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365
F-box_FBXO28 cd22100
F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called ...
 103-133 5.00e-03

F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called FBX28, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It promotes mitotic progression and regulates topoisomerase IIalpha-dependent DNA decatenation. FBXO28 plays a crucial role in the pathogenesis of the 1q41q42 microdeletion syndrome. 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: 438872  Cd Length: 45  Bit Score: 35.60  E-value: 5.00e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 294660155 103 LLNLPTEILLQIFHHLDRKELYSLLTVCHEF 133
Cdd:cd22100    1 LLELPDEIIEKILSYLSYDEISKLRLVCRRF 31
F-box_FBXW9 cd22135
F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, ...
 103-142 5.72e-03

F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, also called F-box and WD-40 domain-containing protein 9, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target 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: 438907  Cd Length: 45  Bit Score: 35.33  E-value: 5.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 294660155 103 LLNLPTEILLQIFHHLDRKELYSLLT-VCHEFADLII-EILW 142
Cdd:cd22135    1 LLSLPPELLLHICSYLDARFVLHVLPlVCKTFRDILSdETTW 42
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 106-138 6.86e-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: 34.64  E-value: 6.86e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 294660155 106 LPTEILLQIFHHLDRKELYSLLTVCHEFADLII 138
Cdd:cd22121    3 LPEEILVHIFRHLSLRDRYAAAQVCKHWREAAL 35
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
84-378 6.93e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.53  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155  84 SSTSNHRNEIQKLNYKNSLLLNLPTEILLQIFHHLDRKELYSLLTVCHEFADLIIEILWFRPNMQNDDSFKKIKTIMEIP 163
Cdd:COG4886    7 SLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 164 KGGTHWDYRSFIKRLNLSFMTKLVD-DDLLKLFVGCPKLERL--TLVNCTKLTY--------SPVTSVLKNCEKLQSIDL 232
Cdd:COG4886   87 LGLTDLGDLTNLTELDLSGNEELSNlTNLESLDLSGNQLTDLpeELANLTNLKEldlsnnqlTDLPEPLGNLTNLKSLDL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294660155 233 --TGVTGIHDDIilalaNNCPRLQGLYAPGCgKVSEdaILKLLKSCPMLKRVKFNGSaNITDrsIEAMHENCKSLVEIDL 310
Cdd:COG4886  167 snNQLTDLPEEL-----GNLTNLKELDLSNN-QITD--LPEPLGNLTNLEELDLSGN-QLTD--LPEPLANLTNLETLDL 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294660155 311 HNCsNVTDkylkLIFL-NLSQLREFRISNaAGVTDrlfelLPSEYYLEKLRIVDITGcNAITDRLIEKL 378
Cdd:COG4886  236 SNN-QLTD----LPELgNLTNLEELDLSN-NQLTD-----LPPLANLTNLKTLDLSN-NQLTDLKLKEL 292
 
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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