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Conserved domains on  [gi|1844084097|ref|NP_001369710|]
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F-box/LRR-repeat protein 19 isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHD_FXL19 cd15645
PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19); FBXL19, also termed ...
67-128 4.55e-38

PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19); FBXL19, also termed F-box/LRR-repeat protein 19, is a novel homolog of KDM2A and KDM2B. It belongs to the Skp1-Cullin-F-box (SCF) family of E3 ubiquitin ligases. FBXL19 mediates ubiquitination and interleukin 33 (IL-33)-induced degradation of ST2L receptor in lung epithelia, blocks IL-33-mediated apoptosis, and prevents endotoxin-induced acute lung injury. It also functions as a RhoA antagonist during cell proliferation and cytoskeleton rearrangement, and regulates RhoA ubiquitination and degradation in lung epithelial cells. Moreover, FBXL19 regulates cell migration by targeting Rac1 for its polyubiquitination and proteasomal degradation. It plays an essential role in regulating TGFbeta1-induced E-cadherin down-regulation by mediating Rac3 site-specific ubiquitination and stability. FBXL19 consists of FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain.


:

Pssm-ID: 277115  Cd Length: 62  Bit Score: 134.67  E-value: 4.55e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844084097  67 VCLLCGEAGKEDTVEGEEEKFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRC 128
Cdd:cd15645     1 VCLACGEAGKEDTAEGEEEKFDLSLMECTICNEIIHPGCLKMGKAEGVINAEIPNCWECPKC 62
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
358-400 3.95e-20

F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; The JHDM family includes F-box/LRR-repeat proteins FBXL10, FBXL11 and FBXL19. FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10 (FBL10), JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. FBXL11, also called KDM2A, CXXC8, F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. FBXL19, also called F-box and leucine-rich repeat protein 19, is the substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It acts as a CpG island-binding protein in mouse embryonic stem (ES) cells and has been shown to associate with the CDK-Mediator complex. It promotes H2Bub1 at the promoters of CpG island-containing genes by interacting with RNF20. 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: 438894  Cd Length: 43  Bit Score: 83.86  E-value: 3.95e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1844084097 358 DHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPR 400
Cdd:cd22122     1 NHVLPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 43
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
403-602 1.73e-14

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


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 73.13  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 403 LSRRKSLTPPMLSGVVRRQPRA---LDLSWTGVSKKQLMWLLNrLQGLQELVLSGC-----SWLSVSALGsapLPALRLL 474
Cdd:cd09293     8 LHKLGQITQSNISQLLRILHSGlewLELYMCPISDPPLDQLSN-CNKLKKLILPGSkliddEGLIALAQS---CPNLQVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 475 DLRWIEDVKDSQLRELLLPPPDTkpgQTESRGRLQGvaelrlaGLELTDASLRLLLRHAPQLSALDLSHCaHVGDPSVHL 554
Cdd:cd09293    84 DLRACENITDSGIVALATNCPKL---QTINLGRHRN-------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844084097 555 LTAPTSPlreTLVHLNLAGCHRLTDHCLPL---FRRCPRLRRLDLRSCRQL 602
Cdd:cd09293   153 LASGCSK---SLERLSLNNCRNLTDQSIPAilaSNYFPNLSVLEFRGCPLI 200
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
30-57 1.73e-08

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


:

Pssm-ID: 366873  Cd Length: 48  Bit Score: 50.82  E-value: 1.73e-08
                          10        20
                  ....*....|....*....|....*...
gi 1844084097  30 CGDCHFCRDMKKFGGPGRMKQSCLLRQC 57
Cdd:pfam02008  21 CGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
 
Name Accession Description Interval E-value
PHD_FXL19 cd15645
PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19); FBXL19, also termed ...
67-128 4.55e-38

PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19); FBXL19, also termed F-box/LRR-repeat protein 19, is a novel homolog of KDM2A and KDM2B. It belongs to the Skp1-Cullin-F-box (SCF) family of E3 ubiquitin ligases. FBXL19 mediates ubiquitination and interleukin 33 (IL-33)-induced degradation of ST2L receptor in lung epithelia, blocks IL-33-mediated apoptosis, and prevents endotoxin-induced acute lung injury. It also functions as a RhoA antagonist during cell proliferation and cytoskeleton rearrangement, and regulates RhoA ubiquitination and degradation in lung epithelial cells. Moreover, FBXL19 regulates cell migration by targeting Rac1 for its polyubiquitination and proteasomal degradation. It plays an essential role in regulating TGFbeta1-induced E-cadherin down-regulation by mediating Rac3 site-specific ubiquitination and stability. FBXL19 consists of FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain.


Pssm-ID: 277115  Cd Length: 62  Bit Score: 134.67  E-value: 4.55e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844084097  67 VCLLCGEAGKEDTVEGEEEKFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRC 128
Cdd:cd15645     1 VCLACGEAGKEDTAEGEEEKFDLSLMECTICNEIIHPGCLKMGKAEGVINAEIPNCWECPKC 62
PHD_4 pfam16866
PHD-finger;
62-129 4.63e-29

PHD-finger;


Pssm-ID: 465288  Cd Length: 66  Bit Score: 109.75  E-value: 4.63e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844084097  62 LPHTAVCLLCGEAGKEDTVEGEEekFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRCT 129
Cdd:pfam16866   1 LPVTAVCIFCGEDGWEDPPEESE--TPSELMECSICYEIVHPQCAKEQNGEGVVNDDLPNSWECPKCC 66
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
358-400 3.95e-20

F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; The JHDM family includes F-box/LRR-repeat proteins FBXL10, FBXL11 and FBXL19. FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10 (FBL10), JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. FBXL11, also called KDM2A, CXXC8, F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. FBXL19, also called F-box and leucine-rich repeat protein 19, is the substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It acts as a CpG island-binding protein in mouse embryonic stem (ES) cells and has been shown to associate with the CDK-Mediator complex. It promotes H2Bub1 at the promoters of CpG island-containing genes by interacting with RNF20. 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: 438894  Cd Length: 43  Bit Score: 83.86  E-value: 3.95e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1844084097 358 DHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPR 400
Cdd:cd22122     1 NHVLPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
403-602 1.73e-14

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 73.13  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 403 LSRRKSLTPPMLSGVVRRQPRA---LDLSWTGVSKKQLMWLLNrLQGLQELVLSGC-----SWLSVSALGsapLPALRLL 474
Cdd:cd09293     8 LHKLGQITQSNISQLLRILHSGlewLELYMCPISDPPLDQLSN-CNKLKKLILPGSkliddEGLIALAQS---CPNLQVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 475 DLRWIEDVKDSQLRELLLPPPDTkpgQTESRGRLQGvaelrlaGLELTDASLRLLLRHAPQLSALDLSHCaHVGDPSVHL 554
Cdd:cd09293    84 DLRACENITDSGIVALATNCPKL---QTINLGRHRN-------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844084097 555 LTAPTSPlreTLVHLNLAGCHRLTDHCLPL---FRRCPRLRRLDLRSCRQL 602
Cdd:cd09293   153 LASGCSK---SLERLSLNNCRNLTDQSIPAilaSNYFPNLSVLEFRGCPLI 200
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
30-57 1.73e-08

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 50.82  E-value: 1.73e-08
                          10        20
                  ....*....|....*....|....*...
gi 1844084097  30 CGDCHFCRDMKKFGGPGRMKQSCLLRQC 57
Cdd:pfam02008  21 CGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
F-box-like pfam12937
F-box-like; This is an F-box-like family.
361-402 7.31e-08

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 49.02  E-value: 7.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRMD 402
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
425-606 1.28e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.09  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 425 LDLSWTGVSkkQLMWLLNRLQGLQELVLSGCSwlsVSALGS--APLPALRLLDLRwiedvkDSQLRELllpppdtkpgqT 502
Cdd:COG4886   118 LDLSGNQLT--DLPEELANLTNLKELDLSNNQ---LTDLPEplGNLTNLKSLDLS------NNQLTDL-----------P 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 503 ESRGRLQGVAELRLAGLELTDasLRLLLRHAPQLSALDLSHCAhvgdpsVHLLTAPTSPLREtLVHLNLAGChRLTDhcL 582
Cdd:COG4886   176 EELGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQ------LTDLPEPLANLTN-LETLDLSNN-QLTD--L 243
                         170       180
                  ....*....|....*....|....*.
gi 1844084097 583 PLFRRCPRLRRLDLRSCR--QLSPEA 606
Cdd:COG4886   244 PELGNLTNLEELDLSNNQltDLPPLA 269
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
588-611 1.35e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 36.23  E-value: 1.35e-03
                           10        20
                   ....*....|....*....|....
gi 1844084097  588 CPRLRRLDLRSCRQLSPEACARLA 611
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
FBOX smart00256
A Receptor for Ubiquitination Targets;
361-388 6.01e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 34.72  E-value: 6.01e-03
                           10        20
                   ....*....|....*....|....*...
gi 1844084097  361 LPRAAWLRVFQHLGPRELCICMRVCRTW 388
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKW 28
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
566-603 6.10e-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: 34.91  E-value: 6.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 566 LVHLNLAGChRLTDhcLPLFRRCPRLRRLDLRSCRQLS 603
Cdd:pfam12799   3 LEVLDLSNN-QITD--IPPLAKLPNLETLDLSGNNKIT 37
 
Name Accession Description Interval E-value
PHD_FXL19 cd15645
PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19); FBXL19, also termed ...
67-128 4.55e-38

PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19); FBXL19, also termed F-box/LRR-repeat protein 19, is a novel homolog of KDM2A and KDM2B. It belongs to the Skp1-Cullin-F-box (SCF) family of E3 ubiquitin ligases. FBXL19 mediates ubiquitination and interleukin 33 (IL-33)-induced degradation of ST2L receptor in lung epithelia, blocks IL-33-mediated apoptosis, and prevents endotoxin-induced acute lung injury. It also functions as a RhoA antagonist during cell proliferation and cytoskeleton rearrangement, and regulates RhoA ubiquitination and degradation in lung epithelial cells. Moreover, FBXL19 regulates cell migration by targeting Rac1 for its polyubiquitination and proteasomal degradation. It plays an essential role in regulating TGFbeta1-induced E-cadherin down-regulation by mediating Rac3 site-specific ubiquitination and stability. FBXL19 consists of FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain.


Pssm-ID: 277115  Cd Length: 62  Bit Score: 134.67  E-value: 4.55e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844084097  67 VCLLCGEAGKEDTVEGEEEKFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRC 128
Cdd:cd15645     1 VCLACGEAGKEDTAEGEEEKFDLSLMECTICNEIIHPGCLKMGKAEGVINAEIPNCWECPKC 62
PHD_KDM2B cd15644
PHD finger found in Lysine-specific demethylase 2B (KDM2B); KDM2B, also termed Ndy1, or ...
67-128 1.29e-32

PHD finger found in Lysine-specific demethylase 2B (KDM2B); KDM2B, also termed Ndy1, or CXXC-type zinc finger protein 2, or F-box and leucine-rich (LRR) repeat protein 10 (FBXL10), or F-box protein FBL10, or JmjC domain-containing histone demethylation protein 1B (Jhdm1b), or Jumonji domain-containing EMSY-interactor methyltransferase motif protein (Protein JEMMA), or [Histone-H3]-lysine-36 demethylase 1B, is a ubiquitously expressed histone H3 lysine 4 (H3K4me2) or histone H3 lysine 36 (H3K36me2) demethylase that functions as a regulator of chemokine expression, cellular morphology, and the metabolome of fibroblasts. It regulates the differentiation of Mesenchymal Stem Cells (MSCs) and has been implicated in cell cycle regulation by de-repressing cyclin-dependent kinase inhibitor 2B (CDKN2B or p15INK4B). It also plays a role in recruiting polycomb repressive complex 1 (PRC1) to CpG islands (CGIs) of developmental genes and regulates lysine 119 monoubiquitylation on H2A (H2AK119ub1) in embryonic stem cells (ESCs). Moreover, it acts as an oncogene that plays a critical role in leukemia development and maintenance. KDM2B consists of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain.


Pssm-ID: 277114  Cd Length: 62  Bit Score: 119.69  E-value: 1.29e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844084097  67 VCLLCGEAGKEDTVEGEEEKFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRC 128
Cdd:cd15644     1 VCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKVKESDGVVNDELPNCWECPKC 62
PHD_4 pfam16866
PHD-finger;
62-129 4.63e-29

PHD-finger;


Pssm-ID: 465288  Cd Length: 66  Bit Score: 109.75  E-value: 4.63e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844084097  62 LPHTAVCLLCGEAGKEDTVEGEEekFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRCT 129
Cdd:pfam16866   1 LPVTAVCIFCGEDGWEDPPEESE--TPSELMECSICYEIVHPQCAKEQNGEGVVNDDLPNSWECPKCC 66
PHD_KDM2A_2B cd15555
PHD finger found in Lysine-specific demethylase KDM2A, KDM2B, and similar proteins; This ...
67-128 5.08e-23

PHD finger found in Lysine-specific demethylase KDM2A, KDM2B, and similar proteins; This family includes KDM2A, KDM2B, and F-box and leucine-rich repeat protein 19 (FBXL19). KDM2A is a ubiquitously expressed histone H3 lysine 36 (H3K36) demethylase that has been implicated in gene silencing, cell cycle, cell growth, and cancer development. KDM2B is a ubiquitously expressed histone H3 lysine 4 (H3K4me2) or histone H3 lysine 36 (H3K36me2) demethylase that functions as a regulator of chemokine expression, cellular morphology, and the metabolome of fibroblasts. Both KDM2A and KDM2B belong to the JmjC-domain-containing histone demethylase family. They consist of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain. FBXL19 belongs to the Skp1-Cullin-F-box (SCF) family of E3 ubiquitin ligases. It mediates ubiquitination and interleukin 33 (IL-33)-induced degradation of ST2L receptor in lung epithelia, blocks IL-33-mediated apoptosis, and prevents endotoxin-induced acute lung injury. FBXL19 consists of FBXHA and FBXHB domains, similar to KDM2A and KDM2B.


Pssm-ID: 277030  Cd Length: 55  Bit Score: 92.08  E-value: 5.08e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844084097  67 VCLLCGEAGKEDTvegeeekFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRC 128
Cdd:cd15555     1 VCLICGEDGKEDE-------FETTLMECSICWEIVHPECLKEQGEGGVVNEDLPNSWECPKC 55
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
358-400 3.95e-20

F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; The JHDM family includes F-box/LRR-repeat proteins FBXL10, FBXL11 and FBXL19. FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10 (FBL10), JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. FBXL11, also called KDM2A, CXXC8, F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. FBXL19, also called F-box and leucine-rich repeat protein 19, is the substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It acts as a CpG island-binding protein in mouse embryonic stem (ES) cells and has been shown to associate with the CDK-Mediator complex. It promotes H2Bub1 at the promoters of CpG island-containing genes by interacting with RNF20. 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: 438894  Cd Length: 43  Bit Score: 83.86  E-value: 3.95e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1844084097 358 DHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPR 400
Cdd:cd22122     1 NHVLPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 43
PHD_KDM2A cd15643
PHD finger found in Lysine-specific demethylase 2A (KDM2A); KDM2A, also termed CXXC-type zinc ...
68-128 2.15e-18

PHD finger found in Lysine-specific demethylase 2A (KDM2A); KDM2A, also termed CXXC-type zinc finger protein 8, or F-box and leucine-rich repeat protein 11 (FBXL11), or F-box protein FBL7, or F-box protein Lilina, or F-box/LRR-repeat protein 11, or JmjC domain-containing histone demethylation protein 1A (Jhdm1a), or [Histone-H3]-lysine-36 demethylase 1A, is a ubiquitously expressed histone H3 lysine 36 (H3K36) demethylase that has been implicated in gene silencing, cell cycle, cell growth, and cancer development. It acts as a key negative regulator of gluconeogenic gene expression and plays a critical role in the invasiveness, proliferation, and anchorage-independent growth of non-small cell lung cancer (NSCLC) cells, as well as in the osteo/dentinogenic differentiation of Mesenchymal stem cells (MSCs). It regulates rRNA transcription in response to starvation. Meanwhile, it is a negative regulator of NFkappaB. Moreover, KDM2A is a heterochromatin-associated and HP1-interacting protein that promotes HP1 localization to chromatin. It is specifically recruited to CpG islands to define a unique chromatin architecture, which requires direct and specific interaction with linker DNA. It also functions as a H3K4 demethylase that regulates cell proliferation through p15 (INK4B) and p27 (Kip1) in stem cells from apical papilla (SCAPs). KDM2A belongs to the JmjC-domain-containing histone demethylase family. KDM2A consists of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain.


Pssm-ID: 277113  Cd Length: 57  Bit Score: 79.29  E-value: 2.15e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844084097  68 CLLCGEAGKEDTVEGEEEKfglsLMECTICNEIVHPGCLKMgKAEGVINAEIPNCWECPRC 128
Cdd:cd15643     2 CALCGEVDQNEDTQDFEKK----LMECCICNEIVHPGCLQM-DGEGLLNDELPNCWECPKC 57
F-box_FBXL10 cd22180
F-box domain found in F-box/LRR-repeat protein 10 (FBXL10) and similar proteins; FBXL10 is ...
356-400 3.91e-18

F-box domain found in F-box/LRR-repeat protein 10 (FBXL10) and similar proteins; FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10, F-box protein FBL10, JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as 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: 438951  Cd Length: 45  Bit Score: 78.05  E-value: 3.91e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1844084097 356 GSDHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPR 400
Cdd:cd22180     1 GAAHVMQREVWMAVFSYLSHRDLCVCMRVCRTWNRWCCDKRLWTR 45
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
403-602 1.73e-14

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 73.13  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 403 LSRRKSLTPPMLSGVVRRQPRA---LDLSWTGVSKKQLMWLLNrLQGLQELVLSGC-----SWLSVSALGsapLPALRLL 474
Cdd:cd09293     8 LHKLGQITQSNISQLLRILHSGlewLELYMCPISDPPLDQLSN-CNKLKKLILPGSkliddEGLIALAQS---CPNLQVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 475 DLRWIEDVKDSQLRELLLPPPDTkpgQTESRGRLQGvaelrlaGLELTDASLRLLLRHAPQLSALDLSHCaHVGDPSVHL 554
Cdd:cd09293    84 DLRACENITDSGIVALATNCPKL---QTINLGRHRN-------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844084097 555 LTAPTSPlreTLVHLNLAGCHRLTDHCLPL---FRRCPRLRRLDLRSCRQL 602
Cdd:cd09293   153 LASGCSK---SLERLSLNNCRNLTDQSIPAilaSNYFPNLSVLEFRGCPLI 200
F-box_FBXL11 cd22181
F-box domain found in F-box/LRR-repeat protein 11 (FBXL11) and similar proteins; FBXL11, also ...
355-400 2.77e-13

F-box domain found in F-box/LRR-repeat protein 11 (FBXL11) and similar proteins; FBXL11, also called lysine-specific demethylase 2A (KDM2A), CXXC-type zinc finger protein (CXXC8), F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. 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: 438952  Cd Length: 47  Bit Score: 64.52  E-value: 2.77e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1844084097 355 AGSDHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPR 400
Cdd:cd22181     2 AGDESWMQKDVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 47
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
30-57 1.73e-08

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 50.82  E-value: 1.73e-08
                          10        20
                  ....*....|....*....|....*...
gi 1844084097  30 CGDCHFCRDMKKFGGPGRMKQSCLLRQC 57
Cdd:pfam02008  21 CGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
F-box-like pfam12937
F-box-like; This is an F-box-like family.
361-402 7.31e-08

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 49.02  E-value: 7.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRMD 402
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
359-398 4.93e-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: 46.56  E-value: 4.93e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1844084097 359 HPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22118     2 SSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
425-606 1.28e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.09  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 425 LDLSWTGVSkkQLMWLLNRLQGLQELVLSGCSwlsVSALGS--APLPALRLLDLRwiedvkDSQLRELllpppdtkpgqT 502
Cdd:COG4886   118 LDLSGNQLT--DLPEELANLTNLKELDLSNNQ---LTDLPEplGNLTNLKSLDLS------NNQLTDL-----------P 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 503 ESRGRLQGVAELRLAGLELTDasLRLLLRHAPQLSALDLSHCAhvgdpsVHLLTAPTSPLREtLVHLNLAGChRLTDhcL 582
Cdd:COG4886   176 EELGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQ------LTDLPEPLANLTN-LETLDLSNN-QLTD--L 243
                         170       180
                  ....*....|....*....|....*.
gi 1844084097 583 PLFRRCPRLRRLDLRSCR--QLSPEA 606
Cdd:COG4886   244 PELGNLTNLEELDLSNNQltDLPPLA 269
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
361-398 2.12e-06

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: 44.68  E-value: 2.12e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22120     4 LPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLW 41
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
361-398 2.85e-06

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: 44.19  E-value: 2.85e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22148     5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELW 42
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
361-398 7.36e-06

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


Pssm-ID: 425796  Cd Length: 43  Bit Score: 43.30  E-value: 7.36e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:pfam00646   4 LPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLW 41
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
361-398 9.22e-06

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: 42.72  E-value: 9.22e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22123     4 LPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
361-388 2.39e-05

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438896  Cd Length: 42  Bit Score: 41.55  E-value: 2.39e-05
                          10        20
                  ....*....|....*....|....*...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTW 388
Cdd:cd22124     4 LPRKAALKIFSYLDLRDLARCAQVCRSW 31
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
358-401 4.41e-05

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: 41.21  E-value: 4.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1844084097 358 DHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRM 401
Cdd:cd22134     4 DIQLPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
361-393 5.01e-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: 40.51  E-value: 5.01e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCY 393
Cdd:cd09917     3 LPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
361-401 5.05e-05

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: 41.06  E-value: 5.05e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRM 401
Cdd:cd22132     4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKEL 44
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
367-400 5.28e-05

F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and similar proteins; DmSKP2 is a Drosophila F-box protein that regulates cell proliferation by targeting Dacapo (Dap) for ubiquitination and proteasome-mediated degradation. It plays a role in maintaining diploidy of mitotic cells during development. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438920  Cd Length: 43  Bit Score: 40.82  E-value: 5.28e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1844084097 367 LRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPR 400
Cdd:cd22149    10 LSIFKWLPKKTLARCARVCRRWKRLCFDESLWRR 43
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
361-404 5.72e-05

F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called FBX13, F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438864  Cd Length: 49  Bit Score: 40.87  E-value: 5.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICM-RVCRTWSRWCYDKRLWPRMDLS 404
Cdd:cd22092     5 LPDSILLKIFSYLSLQERCLSAsLVCKYWRDLCLDSQFWKQIDLS 49
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
360-398 1.53e-04

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that 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: 438911  Cd Length: 45  Bit Score: 39.53  E-value: 1.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1844084097 360 PLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22139     3 CLPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLW 41
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
361-402 4.32e-04

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438910  Cd Length: 45  Bit Score: 38.08  E-value: 4.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRMD 402
Cdd:cd22138     4 LPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTVD 45
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
359-398 6.33e-04

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: 37.78  E-value: 6.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1844084097 359 HPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22115     5 KKLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNW 44
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
521-603 8.30e-04

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: 41.16  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084097 521 LTDASLRLLLRHAP-QLSALDLSHCAhVGDPSVHLLTAPTSplretLVHLNLAGCHRLTDHCL-PLFRRCPRLRRLDLRS 598
Cdd:cd09293    14 ITQSNISQLLRILHsGLEWLELYMCP-ISDPPLDQLSNCNK-----LKKLILPGSKLIDDEGLiALAQSCPNLQVLDLRA 87

                  ....*
gi 1844084097 599 CRQLS 603
Cdd:cd09293    88 CENIT 92
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
588-611 1.35e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 36.23  E-value: 1.35e-03
                           10        20
                   ....*....|....*....|....
gi 1844084097  588 CPRLRRLDLRSCRQLSPEACARLA 611
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
F-box_FBXO16 cd22172
F-box domain found in F-box only protein 16 (FBXO16) and similar proteins; FBXO16, also called ...
361-398 4.38e-03

F-box domain found in F-box only protein 16 (FBXO16) and similar proteins; FBXO16, also called FBX16, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It functions as a tumor suppressor by attenuating nuclear beta-catenin function. 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: 438943  Cd Length: 55  Bit Score: 35.72  E-value: 4.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22172     9 LPRVLSLYIFSFLDPRSLCRCAQVCWYWKYLTELDQLW 46
FBOX smart00256
A Receptor for Ubiquitination Targets;
361-388 6.01e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 34.72  E-value: 6.01e-03
                           10        20
                   ....*....|....*....|....*...
gi 1844084097  361 LPRAAWLRVFQHLGPRELCICMRVCRTW 388
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKW 28
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
566-603 6.10e-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: 34.91  E-value: 6.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 566 LVHLNLAGChRLTDhcLPLFRRCPRLRRLDLRSCRQLS 603
Cdd:pfam12799   3 LEVLDLSNN-QITD--IPPLAKLPNLETLDLSGNNKIT 37
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
359-401 6.28e-03

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. 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: 438863  Cd Length: 45  Bit Score: 35.09  E-value: 6.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1844084097 359 HPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRM 401
Cdd:cd22091     2 EELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRL 44
F-box_FBXO16-like cd22094
F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 ...
361-398 8.44e-03

F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; This family includes FBXO16 and ECT2L. FBXO16, also called FBX16, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It functions as a tumor suppressor by attenuating nuclear beta-catenin function. ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438866  Cd Length: 49  Bit Score: 34.73  E-value: 8.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1844084097 361 LPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLW 398
Cdd:cd22094     6 LPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELW 43
 
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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