AT-rich interactive domain-containing protein arid-1 [Caenorhabditis elegans]
Protein Classification
ARID/BRIGHT DNA-binding domain-containing protein( domain architecture ID 10475762)
ARID (AT-rich interactive domain)/BRIGHT DNA-binding domain-containing protein similar to Caenorhabditis elegans AT-rich interactive domain-containing protein ARID-1
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| ARID | pfam01388 | ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ... |
2-77 | 5.74e-18 | ||
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, and also known as the BRIGHT domain. : Pssm-ID: 460187 Cd Length: 87 Bit Score: 79.59 E-value: 5.74e-18
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| Name | Accession | Description | Interval | E-value | ||
| ARID | pfam01388 | ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ... |
2-77 | 5.74e-18 | ||
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, and also known as the BRIGHT domain. Pssm-ID: 460187 Cd Length: 87 Bit Score: 79.59 E-value: 5.74e-18
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| ARID | smart01014 | ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction ... |
1-77 | 7.11e-17 | ||
ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction domain) family of DNA-binding proteins are found in fungi and invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative transcriptional regulation and a likely involvement in the modification of chromatin structure. The basic structure of the ARID domain domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes: Minimal ARID proteins that consist of a core domain formed by six alpha helices; ARID proteins that supplement the core domain with an N-terminal alpha-helix; and Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini. Pssm-ID: 198082 [Multi-domain] Cd Length: 88 Bit Score: 76.50 E-value: 7.11e-17
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| ARID | cd16100 | ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of ... |
1-77 | 3.09e-15 | ||
ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of transcription factors, found in a broad array of organisms from fungi to mammals, is characterized by a highly conserved, helix-turn-helix DNA binding domain that binds to the major groove of DNA. The ARID domain, also called BRIGHT, was first identified in the mouse B-cell-specific transcription factor Bright and in the product of the dead ringer (dri) gene of Drosophila melanogaster. ARID family members are implicated in normal development, differentiation, cell cycle regulation, transcriptional activation and chromatin remodeling. Different family members exhibit different DNA-binding properties. Drosophila Dri, mammalian ARID3A/3B/3C and ARID5A/5B, selectively bind AT-rich sites. However, ARID1A/1B, Drosophila Osa, yeast SWI1, ARID2, ARID4A/4B, JARID1A/1B/1C/1D, and JARID2, bind DNA without sequence specificity. Pssm-ID: 350627 Cd Length: 87 Bit Score: 71.62 E-value: 3.09e-15
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| Name | Accession | Description | Interval | E-value | ||
| ARID | pfam01388 | ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ... |
2-77 | 5.74e-18 | ||
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, and also known as the BRIGHT domain. Pssm-ID: 460187 Cd Length: 87 Bit Score: 79.59 E-value: 5.74e-18
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| ARID | smart01014 | ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction ... |
1-77 | 7.11e-17 | ||
ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction domain) family of DNA-binding proteins are found in fungi and invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative transcriptional regulation and a likely involvement in the modification of chromatin structure. The basic structure of the ARID domain domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes: Minimal ARID proteins that consist of a core domain formed by six alpha helices; ARID proteins that supplement the core domain with an N-terminal alpha-helix; and Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini. Pssm-ID: 198082 [Multi-domain] Cd Length: 88 Bit Score: 76.50 E-value: 7.11e-17
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| ARID | cd16100 | ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of ... |
1-77 | 3.09e-15 | ||
ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of transcription factors, found in a broad array of organisms from fungi to mammals, is characterized by a highly conserved, helix-turn-helix DNA binding domain that binds to the major groove of DNA. The ARID domain, also called BRIGHT, was first identified in the mouse B-cell-specific transcription factor Bright and in the product of the dead ringer (dri) gene of Drosophila melanogaster. ARID family members are implicated in normal development, differentiation, cell cycle regulation, transcriptional activation and chromatin remodeling. Different family members exhibit different DNA-binding properties. Drosophila Dri, mammalian ARID3A/3B/3C and ARID5A/5B, selectively bind AT-rich sites. However, ARID1A/1B, Drosophila Osa, yeast SWI1, ARID2, ARID4A/4B, JARID1A/1B/1C/1D, and JARID2, bind DNA without sequence specificity. Pssm-ID: 350627 Cd Length: 87 Bit Score: 71.62 E-value: 3.09e-15
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| ARID_Swi1p-like | cd16871 | ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and ... |
2-74 | 9.96e-11 | ||
ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and similar proteins; Saccharomyces cerevisiae Swi1p, also called SWI/SNF chromatin-remodeling complex subunit SWI1, regulatory protein GAM3, or transcription regulatory protein ADR6, is a transcription regulatory protein that is a subunit of the SWI/SNF complex, which plays critical roles in the regulation of gene transcription and expression. It can exist as a prion, [SWI(+)], which demonstrates a link between prionogenesis and global transcriptional regulation. Swi1p contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT) that binds DNA nonspecifically. This subfamily also includes Schizosaccharomyces pombe SWI/SNF chromatin-remodeling complex subunit sol1 (sol1p, also known as switch one-like protein). sol1p is a homolog of S. cerevisiae Swi1p and is also a part of SWI/SNF chromatin-remodeling complex. Pssm-ID: 350635 Cd Length: 90 Bit Score: 59.19 E-value: 9.96e-11
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| BRIGHT | smart00501 | BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a ... |
1-78 | 7.74e-07 | ||
BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a helix-turn-helix structure Pssm-ID: 128777 [Multi-domain] Cd Length: 93 Bit Score: 48.04 E-value: 7.74e-07
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| ARID_ARID2 | cd16866 | ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and ... |
2-77 | 2.09e-06 | ||
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and similar proteins; ARID2, also called BRG1-associated factor 200 (BAF200) or zinc finger protein with activation potential (Zipzap/p200), is a novel serum response factor (SRF)-binding protein with multiple conserved domains, including an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), RFX DNA-binding domain, a glutamine-rich domain, and two C2H2 zinc fingers. It binds DNA without sequence specificity. ARID2 is an intrinsic subunit of PBAF (SWI/SNF-B) remodeling complex, which needs ARID2 to play an essential role in promoting osteoblast differentiation, maintaining cellular identity and activating tissue-specific gene expression. Moreover, ARID2 may function as a tumor suppressor in many cancers. It may also serve as a transcription co-activator for the regulation of cardiac gene expression, and is required for heart morphogenesis and coronary artery development. Pssm-ID: 350630 Cd Length: 88 Bit Score: 46.87 E-value: 2.09e-06
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| ARID_JARD2 | cd16870 | ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and ... |
10-77 | 1.04e-03 | ||
ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and similar proteins; JARID2, also called protein Jumonji, is a DNA-binding protein that contains both the Jumonji C (JmjC) domain and AT-rich DNA-interacting domain (ARID, also known as BRIGHT). It is an interacting component of Polycomb repressive complex-2 (PRC2) that catalyzes methylation of lysine 27 of histone H3 (H3K27) and regulates important gene expression patterns during development. It exhibits nucleosome-binding activity that contributes to PRC2 stimulation. However, unlike other JmjC domain-containing proteins, JARID2 is catalytically inactive due to the lack of conserved residues essential for histone demethylase activity. JARID2 is also involved in transforming growth factor-beta (TGF-beta)-induced epithelial-mesenchymal transition (EMT) of lung and colon cancer cell lines through the modulation of histone H3K27 methylation. Moreover, JARID2 is a part of GLP- and G9a-containing protein complex that promotes lysine 9 on histone H3 (H3K9) methylation on the cyclin D1 promoter and silences the expression of cyclin D1 and other cell cycle genes. It functions as a transcriptional repressor that plays critical roles in embryonic development including heart development in mice, and regulates cardiomyocyte proliferation via interaction with retinoblastoma protein (Rb), one of the master regulatory genes of the cell cycle. Furthermore, JARID2 acts as a transcriptional repressor of target genes, including Notch1. It directly binds to SETDB1 (SET domain, bifurcated 1) to form a complex that plays an important role in a novel process involving the modification of H3K9 methylation during heart development. Meanwhile, JARID2 is a key transcriptional repressor that plays a role in invariant natural killer T (iNKT) cell maturation. It regulates promyelocytic leukemia zinc finger (PLZF) expression by linking T-cell receptor (TCR) signaling to H3K9me3. JARID2 polymorphisms are associated with non-syndromic orofacial clefts (NSOC) susceptibility. Pssm-ID: 350634 Cd Length: 112 Bit Score: 39.51 E-value: 1.04e-03
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