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Conserved domains on  [gi|39963079|gb|AAH64360|]
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F-box and leucine-rich repeat protein 11 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CTD_KDM2A cd21784
C-terminal domain found in Lysine-specific demethylase 2A; Lysine-specific demethylase 2A ...
450-517 8.85e-39

C-terminal domain found in Lysine-specific demethylase 2A; Lysine-specific demethylase 2A (KDM2A) is also called CXXC-type zinc finger protein 8, F-box and leucine-rich repeat protein 11 (FBXL11), F-box protein FBL7, F-box protein Lilina, F-box/LRR-repeat protein 11, JmjC domain-containing histone demethylation protein 1A (Jhdm1a), or [Histone-H3]-lysine-36 demethylase 1A. It 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). KDM2A regulates rRNA transcription in response to starvation and functions as a negative regulator of NF-kappaB. It is a heterochromatin-associated and HP1-interacting protein that promotes Heterochromatin Protein 1 (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 domains (JmjN and JmjC), a CXXC zinc-finger domain, a plant homeodomain (PHD) finger, an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain. This model corresponds to a small conserved region in KDM2A between the JmjC domain and the CXXC zinc-finger domain, which has been called the C-terminal domain by literature.


:

Pssm-ID: 412025  Cd Length: 68  Bit Score: 138.33  E-value: 8.85e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39963079  450 QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWP 517
Cdd:cd21784    1 QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEEHANDDPKLALTGVPIVQWP 68
PHD_KDM2A cd15643
PHD finger found in Lysine-specific demethylase 2A (KDM2A); KDM2A, also termed CXXC-type zinc ...
619-675 2.52e-38

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: 136.69  E-value: 2.52e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079  619 TCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEGLLNEELPNCWECPKC 675
Cdd:cd15643    1 TCALCGEVDQNEDTQDFEKKLMECCICNEIVHPGCLQMDGEGLLNDELPNCWECPKC 57
F-box_FBXL11 cd22181
F-box domain found in F-box/LRR-repeat protein 11 (FBXL11) and similar proteins; FBXL11, also ...
886-932 1.16e-27

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: 106.13  E-value: 1.16e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 39963079  886 QDGDESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 932
Cdd:cd22181    1 QAGDESWMQKDVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 47
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
576-609 5.69e-11

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: 58.52  E-value: 5.69e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 39963079    576 ACVQGE-CGVCHYCRDMKKFGGPGRMKQSCVLRQC 609
Cdd:pfam02008   14 GCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
199-299 1.02e-10

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member pfam02373:

Pssm-ID: 477354  Cd Length: 114  Bit Score: 60.00  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079    199 YCLMSVRGCYTDFHVDFGGT-SVWYHIHQGGKVFWLIPP-TAHNLELYENWLLSGKQGD--IFLGDRVSDCQ-------- 266
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLySINYLHFGAPKVWYIIPPeYAEKFEKVLSDHFGGEQPDdlLHLNTIISPKQlrengipv 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 39963079    267 -RIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNF 299
Cdd:pfam02373   81 yRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JHD super family cl39304
Jumonji helical domain; This 4-helix bundle domain is associated with the Jumonji domain ...
304-339 3.33e-10

Jumonji helical domain; This 4-helix bundle domain is associated with the Jumonji domain pfam02373.


The actual alignment was detected with superfamily member pfam17811:

Pssm-ID: 465515  Cd Length: 104  Bit Score: 58.14  E-value: 3.33e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 39963079    304 NIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLER 339
Cdd:pfam17811    2 NIEMQLRAYEIEKRLKTPDLFKFPNFETICWYVAKH 37
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
932-1138 5.03e-09

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


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 58.11  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079  932 KIDLSRCKAIVPQALSGIIKRQPVSLDL-SWTNISKKQLTWLVNRLPGLKDLLLAGC---SWSAVSALSTSsCPLLRTLD 1007
Cdd:cd09293   32 WLELYMCPISDPPLDQLSNCNKLKKLILpGSKLIDDEGLIALAQSCPNLQVLDLRACeniTDSGIVALATN-CPKLQTIN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079 1008 LRWAVG---IKDPQIRDLltppadkpGQDNRsklrNMTDFRLAGLDITDATLR-LIIRHMPLLSRLDLSHCSHLTDQSsn 1083
Cdd:cd09293  111 LGRHRNghlITDVSLSAL--------GKNCT----FLQTVGFAGCDVTDKGVWeLASGCSKSLERLSLNNCRNLTDQS-- 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 39963079 1084 lLTAVGSSTRYS-LTELNMAGCNKLTDqtliyLRRIANVTLIDLRGCKQITRKACE 1138
Cdd:cd09293  177 -IPAILASNYFPnLSVLEFRGCPLITD-----FSRIILFKLWQPRLNKPILVEWCE 226
 
Name Accession Description Interval E-value
CTD_KDM2A cd21784
C-terminal domain found in Lysine-specific demethylase 2A; Lysine-specific demethylase 2A ...
450-517 8.85e-39

C-terminal domain found in Lysine-specific demethylase 2A; Lysine-specific demethylase 2A (KDM2A) is also called CXXC-type zinc finger protein 8, F-box and leucine-rich repeat protein 11 (FBXL11), F-box protein FBL7, F-box protein Lilina, F-box/LRR-repeat protein 11, JmjC domain-containing histone demethylation protein 1A (Jhdm1a), or [Histone-H3]-lysine-36 demethylase 1A. It 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). KDM2A regulates rRNA transcription in response to starvation and functions as a negative regulator of NF-kappaB. It is a heterochromatin-associated and HP1-interacting protein that promotes Heterochromatin Protein 1 (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 domains (JmjN and JmjC), a CXXC zinc-finger domain, a plant homeodomain (PHD) finger, an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain. This model corresponds to a small conserved region in KDM2A between the JmjC domain and the CXXC zinc-finger domain, which has been called the C-terminal domain by literature.


Pssm-ID: 412025  Cd Length: 68  Bit Score: 138.33  E-value: 8.85e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39963079  450 QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWP 517
Cdd:cd21784    1 QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEEHANDDPKLALTGVPIVQWP 68
PHD_KDM2A cd15643
PHD finger found in Lysine-specific demethylase 2A (KDM2A); KDM2A, also termed CXXC-type zinc ...
619-675 2.52e-38

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: 136.69  E-value: 2.52e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079  619 TCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEGLLNEELPNCWECPKC 675
Cdd:cd15643    1 TCALCGEVDQNEDTQDFEKKLMECCICNEIVHPGCLQMDGEGLLNDELPNCWECPKC 57
F-box_FBXL11 cd22181
F-box domain found in F-box/LRR-repeat protein 11 (FBXL11) and similar proteins; FBXL11, also ...
886-932 1.16e-27

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: 106.13  E-value: 1.16e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 39963079  886 QDGDESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 932
Cdd:cd22181    1 QAGDESWMQKDVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 47
PHD_4 pfam16866
PHD-finger;
614-676 4.05e-27

PHD-finger;


Pssm-ID: 465288  Cd Length: 66  Bit Score: 105.13  E-value: 4.05e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39963079    614 LPHSVTCSLCGEVDQNE--ETQDFEKKLMECCICNEIVHPGCLQM-DGEGLLNEELPNCWECPKCY 676
Cdd:pfam16866    1 LPVTAVCIFCGEDGWEDppEESETPSELMECSICYEIVHPQCAKEqNGEGVVNDDLPNSWECPKCC 66
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
576-609 5.69e-11

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: 58.52  E-value: 5.69e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 39963079    576 ACVQGE-CGVCHYCRDMKKFGGPGRMKQSCVLRQC 609
Cdd:pfam02008   14 GCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
199-299 1.02e-10

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 60.00  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079    199 YCLMSVRGCYTDFHVDFGGT-SVWYHIHQGGKVFWLIPP-TAHNLELYENWLLSGKQGD--IFLGDRVSDCQ-------- 266
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLySINYLHFGAPKVWYIIPPeYAEKFEKVLSDHFGGEQPDdlLHLNTIISPKQlrengipv 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 39963079    267 -RIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNF 299
Cdd:pfam02373   81 yRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JHD pfam17811
Jumonji helical domain; This 4-helix bundle domain is associated with the Jumonji domain ...
304-339 3.33e-10

Jumonji helical domain; This 4-helix bundle domain is associated with the Jumonji domain pfam02373.


Pssm-ID: 465515  Cd Length: 104  Bit Score: 58.14  E-value: 3.33e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 39963079    304 NIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLER 339
Cdd:pfam17811    2 NIEMQLRAYEIEKRLKTPDLFKFPNFETICWYVAKH 37
F-box-like pfam12937
F-box-like; This is an F-box-like family.
896-934 1.06e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 54.80  E-value: 1.06e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 39963079    896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKID 934
Cdd:pfam12937    7 EILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
932-1138 5.03e-09

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 58.11  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079  932 KIDLSRCKAIVPQALSGIIKRQPVSLDL-SWTNISKKQLTWLVNRLPGLKDLLLAGC---SWSAVSALSTSsCPLLRTLD 1007
Cdd:cd09293   32 WLELYMCPISDPPLDQLSNCNKLKKLILpGSKLIDDEGLIALAQSCPNLQVLDLRACeniTDSGIVALATN-CPKLQTIN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079 1008 LRWAVG---IKDPQIRDLltppadkpGQDNRsklrNMTDFRLAGLDITDATLR-LIIRHMPLLSRLDLSHCSHLTDQSsn 1083
Cdd:cd09293  111 LGRHRNghlITDVSLSAL--------GKNCT----FLQTVGFAGCDVTDKGVWeLASGCSKSLERLSLNNCRNLTDQS-- 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 39963079 1084 lLTAVGSSTRYS-LTELNMAGCNKLTDqtliyLRRIANVTLIDLRGCKQITRKACE 1138
Cdd:cd09293  177 -IPAILASNYFPnLSVLEFRGCPLITD-----FSRIILFKLWQPRLNKPILVEWCE 226
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
194-223 2.69e-06

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 45.71  E-value: 2.69e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 39963079     194 PKVQKYCLMSVRGCYTDFHVDFGGTSVWYH 223
Cdd:smart00558   25 PDVGPYLYMGMAGSTTPWHIDDYDLVNYLH 54
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
619-675 5.13e-04

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 38.73  E-value: 5.13e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079     619 TCSLCGEVDQNEEtqdfekkLMECCICNEIVHPGCLQMDGEGLLNEElpnCWECPKC 675
Cdd:smart00249    1 YCSVCGKPDDGGE-------LLQCDGCDRWYHQTCLGPPLLEEEPDG---KWYCPKC 47
 
Name Accession Description Interval E-value
CTD_KDM2A cd21784
C-terminal domain found in Lysine-specific demethylase 2A; Lysine-specific demethylase 2A ...
450-517 8.85e-39

C-terminal domain found in Lysine-specific demethylase 2A; Lysine-specific demethylase 2A (KDM2A) is also called CXXC-type zinc finger protein 8, F-box and leucine-rich repeat protein 11 (FBXL11), F-box protein FBL7, F-box protein Lilina, F-box/LRR-repeat protein 11, JmjC domain-containing histone demethylation protein 1A (Jhdm1a), or [Histone-H3]-lysine-36 demethylase 1A. It 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). KDM2A regulates rRNA transcription in response to starvation and functions as a negative regulator of NF-kappaB. It is a heterochromatin-associated and HP1-interacting protein that promotes Heterochromatin Protein 1 (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 domains (JmjN and JmjC), a CXXC zinc-finger domain, a plant homeodomain (PHD) finger, an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain. This model corresponds to a small conserved region in KDM2A between the JmjC domain and the CXXC zinc-finger domain, which has been called the C-terminal domain by literature.


Pssm-ID: 412025  Cd Length: 68  Bit Score: 138.33  E-value: 8.85e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39963079  450 QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWP 517
Cdd:cd21784    1 QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEEHANDDPKLALTGVPIVQWP 68
PHD_KDM2A cd15643
PHD finger found in Lysine-specific demethylase 2A (KDM2A); KDM2A, also termed CXXC-type zinc ...
619-675 2.52e-38

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: 136.69  E-value: 2.52e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079  619 TCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEGLLNEELPNCWECPKC 675
Cdd:cd15643    1 TCALCGEVDQNEDTQDFEKKLMECCICNEIVHPGCLQMDGEGLLNDELPNCWECPKC 57
CTD_KDM2A_2B-like cd21743
C-terminal domain found in lysine-specific demethylase KDM2A, KDM2B, and similar proteins; ...
451-517 2.18e-30

C-terminal domain found in lysine-specific demethylase KDM2A, KDM2B, and similar proteins; This family includes lysine-specific demethylases KDM2A and KDM2B, as well as Drosophila melanogaster JmjC domain-containing histone demethylation protein 1 (Jhd1). 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. Jhd1, also called lysine (K)-specific demethylase 2 (KDM2), or [Histone-H3]-lysine-36 demethylase 1, is a histone demethylase (EC 1.14.11.27) that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in the histone code. Members in this family belong to the JmjC domain-containing histone demethylase family. They consist of two Jumonji domains (JmjN and JmjC), a CXXC zinc-finger domain, a plant homeodomain (PHD) finger, an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain. This model corresponds to a small conserved region between the JmjC domain and the CXXC zinc-finger domain, which has been called the C-terminal domain by literature.


Pssm-ID: 412023  Cd Length: 67  Bit Score: 114.57  E-value: 2.18e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079  451 VHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWP 517
Cdd:cd21743    1 VHLTQFELEGLKKLVDWLESLPQNKKNVPDLILDPDALLQDLKELLEEHKDDDPSLAITGEPILKWP 67
F-box_FBXL11 cd22181
F-box domain found in F-box/LRR-repeat protein 11 (FBXL11) and similar proteins; FBXL11, also ...
886-932 1.16e-27

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: 106.13  E-value: 1.16e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 39963079  886 QDGDESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 932
Cdd:cd22181    1 QAGDESWMQKDVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 47
PHD_4 pfam16866
PHD-finger;
614-676 4.05e-27

PHD-finger;


Pssm-ID: 465288  Cd Length: 66  Bit Score: 105.13  E-value: 4.05e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39963079    614 LPHSVTCSLCGEVDQNE--ETQDFEKKLMECCICNEIVHPGCLQM-DGEGLLNEELPNCWECPKCY 676
Cdd:pfam16866    1 LPVTAVCIFCGEDGWEDppEESETPSELMECSICYEIVHPQCAKEqNGEGVVNDDLPNSWECPKCC 66
PHD_KDM2A_2B cd15555
PHD finger found in Lysine-specific demethylase KDM2A, KDM2B, and similar proteins; This ...
619-675 9.71e-25

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: 97.86  E-value: 9.71e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 39963079  619 TCSLCGEVDQNEEtqdFEKKLMECCICNEIVHPGCLQMDGEG-LLNEELPNCWECPKC 675
Cdd:cd15555    1 VCLICGEDGKEDE---FETTLMECSICWEIVHPECLKEQGEGgVVNEDLPNSWECPKC 55
CTD_KDM2B cd21785
C-terminal domain found in Lysine-specific demethylase 2B; Lysine-specific demethylase 2B ...
451-517 6.36e-24

C-terminal domain found in Lysine-specific demethylase 2B; Lysine-specific demethylase 2B (KDM2B) is also called Ndy1, CXXC-type zinc finger protein 2, F-box and leucine-rich (LRR) repeat protein 10 (FBXL10), F-box protein FBL10, JmjC domain-containing histone demethylation protein 1B (Jhdm1b), Jumonji domain-containing EMSY-interactor methyltransferase motif protein (protein JEMMA), or [Histone-H3]-lysine-36 demethylase 1B. It 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). KDM2B also acts as an oncogene that plays a critical role in leukemia development and maintenance. It consists of two Jumonji domains (JmjN and JmjC), a CXXC zinc-finger domain, a plant homeodomain (PHD) finger, an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain. This model corresponds to a small conserved region in KDM2B between the JmjC domain and the CXXC zinc-finger domain, which has been called the C-terminal domain by literature.


Pssm-ID: 412026  Cd Length: 67  Bit Score: 96.09  E-value: 6.36e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079  451 VHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWP 517
Cdd:cd21785    1 THLTEFELKGLKALVEKLESLPENKKCVPEGIEDPQALLEDMKNVLKEHADDDPNLAISGVPVVSWP 67
F-box_FBXL10 cd22180
F-box domain found in F-box/LRR-repeat protein 10 (FBXL10) and similar proteins; FBXL10 is ...
888-932 1.97e-21

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: 88.07  E-value: 1.97e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 39963079  888 GDESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 932
Cdd:cd22180    1 GAAHVMQREVWMAVFSYLSHRDLCVCMRVCRTWNRWCCDKRLWTR 45
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
890-931 4.65e-21

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: 86.95  E-value: 4.65e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 39963079  890 ESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWT 931
Cdd:cd22122    1 NHVLPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWK 42
PHD_FXL19 cd15645
PHD finger found in F-box and leucine-rich repeat protein 19 (FBXL19); FBXL19, also termed ...
620-675 9.54e-21

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: 86.91  E-value: 9.54e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39963079  620 CSLCGEVDQNE----ETQDFEKKLMECCICNEIVHPGCLQM-DGEGLLNEELPNCWECPKC 675
Cdd:cd15645    2 CLACGEAGKEDtaegEEEKFDLSLMECTICNEIIHPGCLKMgKAEGVINAEIPNCWECPKC 62
PHD_KDM2B cd15644
PHD finger found in Lysine-specific demethylase 2B (KDM2B); KDM2B, also termed Ndy1, or ...
620-675 1.31e-20

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: 86.57  E-value: 1.31e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39963079  620 CSLCGEVDQNEETQDFEKK----LMECCICNEIVHPGCLQM-DGEGLLNEELPNCWECPKC 675
Cdd:cd15644    2 CLVCGEAGKEDTVEEEEGKfnlmLMECSICNEIIHPGCLKVkESDGVVNDELPNCWECPKC 62
CTD_Jhd1-like cd21783
C-terminal domain found in Drosophila melanogaster JmjC domain-containing histone ...
451-517 3.26e-16

C-terminal domain found in Drosophila melanogaster JmjC domain-containing histone demethylation protein 1 and similar proteins; JmjC domain-containing histone demethylation protein 1 (Jhd1), also called lysine (K)-specific demethylase 2 (KDM2), or [Histone-H3]-lysine-36 demethylase 1, is a histone demethylase (EC 1.14.11.27) that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in the histone code. Jhd1 consists of two Jumonji domains (JmjN and JmjC), a CXXC zinc-finger domain, a plant homeodomain (PHD) finger, an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain. This model corresponds to a small conserved region in Jhd1 between the JmjC domain and the CXXC zinc-finger domain, which has been called the C-terminal domain by literature.


Pssm-ID: 412024  Cd Length: 67  Bit Score: 73.88  E-value: 3.26e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079  451 VHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWP 517
Cdd:cd21783    1 VHLTKQELHGLKAIVMYLHDLPPQKKNVPPLIKDPVALIKDVRSIVERHKKDQPELAITGRPILKWP 67
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
576-609 5.69e-11

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: 58.52  E-value: 5.69e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 39963079    576 ACVQGE-CGVCHYCRDMKKFGGPGRMKQSCVLRQC 609
Cdd:pfam02008   14 GCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
199-299 1.02e-10

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 60.00  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079    199 YCLMSVRGCYTDFHVDFGGT-SVWYHIHQGGKVFWLIPP-TAHNLELYENWLLSGKQGD--IFLGDRVSDCQ-------- 266
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLySINYLHFGAPKVWYIIPPeYAEKFEKVLSDHFGGEQPDdlLHLNTIISPKQlrengipv 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 39963079    267 -RIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNF 299
Cdd:pfam02373   81 yRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JHD pfam17811
Jumonji helical domain; This 4-helix bundle domain is associated with the Jumonji domain ...
304-339 3.33e-10

Jumonji helical domain; This 4-helix bundle domain is associated with the Jumonji domain pfam02373.


Pssm-ID: 465515  Cd Length: 104  Bit Score: 58.14  E-value: 3.33e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 39963079    304 NIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLER 339
Cdd:pfam17811    2 NIEMQLRAYEIEKRLKTPDLFKFPNFETICWYVAKH 37
F-box-like pfam12937
F-box-like; This is an F-box-like family.
896-934 1.06e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 54.80  E-value: 1.06e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 39963079    896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKID 934
Cdd:pfam12937    7 EILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
932-1138 5.03e-09

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 58.11  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079  932 KIDLSRCKAIVPQALSGIIKRQPVSLDL-SWTNISKKQLTWLVNRLPGLKDLLLAGC---SWSAVSALSTSsCPLLRTLD 1007
Cdd:cd09293   32 WLELYMCPISDPPLDQLSNCNKLKKLILpGSKLIDDEGLIALAQSCPNLQVLDLRACeniTDSGIVALATN-CPKLQTIN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079 1008 LRWAVG---IKDPQIRDLltppadkpGQDNRsklrNMTDFRLAGLDITDATLR-LIIRHMPLLSRLDLSHCSHLTDQSsn 1083
Cdd:cd09293  111 LGRHRNghlITDVSLSAL--------GKNCT----FLQTVGFAGCDVTDKGVWeLASGCSKSLERLSLNNCRNLTDQS-- 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 39963079 1084 lLTAVGSSTRYS-LTELNMAGCNKLTDqtliyLRRIANVTLIDLRGCKQITRKACE 1138
Cdd:cd09293  177 -IPAILASNYFPnLSVLEFRGCPLITD-----FSRIILFKLWQPRLNKPILVEWCE 226
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
896-933 1.90e-06

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: 45.70  E-value: 1.90e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKI 933
Cdd:cd22139    7 ELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
896-932 1.97e-06

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: 45.44  E-value: 1.97e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 932
Cdd:cd22149    7 EIILSIFKWLPKKTLARCARVCRRWKRLCFDESLWRR 43
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
194-223 2.69e-06

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 45.71  E-value: 2.69e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 39963079     194 PKVQKYCLMSVRGCYTDFHVDFGGTSVWYH 223
Cdd:smart00558   25 PDVGPYLYMGMAGSTTPWHIDDYDLVNYLH 54
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
896-933 3.44e-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: 45.07  E-value: 3.44e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKI 933
Cdd:cd22120    7 DVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
990-1154 8.74e-06

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: 48.09  E-value: 8.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079  990 SAVSALSTSSCPLLRTLDLRwavgikdpqIRDLLTPPADKpgQDNRSKLRNMTdfrLAG-LDITDATLRLIIRHMPLLSR 1068
Cdd:cd09293   17 SNISQLLRILHSGLEWLELY---------MCPISDPPLDQ--LSNCNKLKKLI---LPGsKLIDDEGLIALAQSCPNLQV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39963079 1069 LDLSHCSHLTDQSsnlLTAVGSSTRYsLTELNM---AGCNKLTDQTLIYL-RRIANVTLIDLRGCkQITRKA-------C 1137
Cdd:cd09293   83 LDLRACENITDSG---IVALATNCPK-LQTINLgrhRNGHLITDVSLSALgKNCTFLQTVGFAGC-DVTDKGvwelasgC 157
                        170
                 ....*....|....*..
gi 39963079 1138 EHFISDLSINSLYCLSD 1154
Cdd:cd09293  158 SKSLERLSLNNCRNLTD 174
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
896-932 1.44e-05

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: 42.91  E-value: 1.44e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 39963079    896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTK 932
Cdd:pfam00646    7 DLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
896-925 1.72e-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: 42.82  E-value: 1.72e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWYKWCC 925
Cdd:cd09917    6 EILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
895-933 1.96e-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: 42.75  E-value: 1.96e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 39963079  895 REVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKI 933
Cdd:cd22134    9 RELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
897-936 7.14e-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: 41.25  E-value: 7.14e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 39963079  897 VWMSVFRYLSRRELCECM-RVCKTWYKWCCDKRLWTKIDLS 936
Cdd:cd22092    9 ILLKIFSYLSLQERCLSAsLVCKYWRDLCLDSQFWKQIDLS 49
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
896-921 1.09e-04

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


Pssm-ID: 438862  Cd Length: 50  Bit Score: 40.80  E-value: 1.09e-04
                         10        20
                 ....*....|....*....|....*.
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWY 921
Cdd:cd22090    8 ELWRLILAYLPVRDLCRCCQVCRAWY 33
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
896-930 1.59e-04

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: 40.01  E-value: 1.59e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLW 930
Cdd:cd22118    7 EIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
619-675 1.83e-04

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 40.38  E-value: 1.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079  619 TCSLCGEVDQNEEtqdfekKLMECCICNEIVHPGCLQMDGEgllNEELPNCWECPKC 675
Cdd:cd15489    1 SCIVCGKGGDLGG------ELLQCDGCGKWFHADCLGPPLS---SFVPNGKWICPVC 48
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
891-930 2.27e-04

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: 39.64  E-value: 2.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 39963079  891 SWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLW 930
Cdd:cd22123    2 DQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
619-675 5.13e-04

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 38.73  E-value: 5.13e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 39963079     619 TCSLCGEVDQNEEtqdfekkLMECCICNEIVHPGCLQMDGEGLLNEElpnCWECPKC 675
Cdd:smart00249    1 YCSVCGKPDDGGE-------LLQCDGCDRWYHQTCLGPPLLEEEPDG---KWYCPKC 47
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
901-930 7.59e-04

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: 38.42  E-value: 7.59e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 39963079  901 VFRYLSRRELCECMRVCKTWYKWCCDKRLW 930
Cdd:cd22148   13 ILSYLSPKELLIASQVSKTWRRLASSNELW 42
F-box_ScDIA2-like cd22142
F-box domain found in Saccharomyces cerevisiae protein Digs into agar protein 2 (ScDIA2) and ...
896-935 1.35e-03

F-box domain found in Saccharomyces cerevisiae protein Digs into agar protein 2 (ScDIA2) and similar proteins; ScDIA2 is a replication origin-binding protein that plays a role in regulating DNA replication. It is a component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which 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: 438914  Cd Length: 48  Bit Score: 37.84  E-value: 1.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDK-RLWTKIDL 935
Cdd:cd22142    8 DILPLIFQKFSTKELITLSHVCSSWRAKILDFpHLWKTVEL 48
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
899-934 1.92e-03

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


Pssm-ID: 438910  Cd Length: 45  Bit Score: 37.31  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 39963079  899 MSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKID 934
Cdd:cd22138   10 LKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTVD 45
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
896-935 5.42e-03

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438889  Cd Length: 47  Bit Score: 36.06  E-value: 5.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 39963079  896 EVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKIDL 935
Cdd:cd22117    7 ELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNL 46
 
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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