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.

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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690195     46 ISLFRPLLDSFLAEFCSAdgFLPLPAMtgEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESY---DSASAKL 122
Cdd:smart00501   3 RVLFLDRLYKFMEERGSP--LKKIPVI--GGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPDTstsAASSLRK 78

                           90
                   ....*....|....*
gi 30690195    123 IYVKYLDAFGRWLNR 137
Cdd:smart00501  79 HYERYLLPYERFLRG 93

BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a helix-turn-helix structure

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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690195     46 ISLFRPLLDSFLAEFCSAdgFLPLPAMtgEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESY---DSASAKL 122
Cdd:smart00501   3 RVLFLDRLYKFMEERGSP--LKKIPVI--GGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPDTstsAASSLRK 78

                           90
                   ....*....|....*
gi 30690195    123 IYVKYLDAFGRWLNR 137
Cdd:smart00501  79 HYERYLLPYERFLRG 93

ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, and also known as the BRIGHT domain.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690195    57 LAEFCSADG--FLPLPAMtgEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESYDSASA---KLIYVKYLDAF 131
Cdd:pfam01388   9 LRKFHEKRGtpLKQIPVI--GGKPVDLYKLYKAVQKLGGYDKVTEKNLWREVAEKLGFPPSAASAAtqlKQIYEKYLLPY 86

BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a helix-turn-helix structure

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690195     46 ISLFRPLLDSFLAEFCSAdgFLPLPAMtgEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESY---DSASAKL 122
Cdd:smart00501   3 RVLFLDRLYKFMEERGSP--LKKIPVI--GGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPDTstsAASSLRK 78

                           90
                   ....*....|....*
gi 30690195    123 IYVKYLDAFGRWLNR 137
Cdd:smart00501  79 HYERYLLPYERFLRG 93

ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, and also known as the BRIGHT domain.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690195    57 LAEFCSADG--FLPLPAMtgEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESYDSASA---KLIYVKYLDAF 131
Cdd:pfam01388   9 LRKFHEKRGtpLKQIPVI--GGKPVDLYKLYKAVQKLGGYDKVTEKNLWREVAEKLGFPPSAASAAtqlKQIYEKYLLPY 86

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690195  57 LAEFCSADG--FLPLPAMtgEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGL--ESYDSASAKL--IYVKYLDA 130
Cdd:cd16871  10 LREFMAKRGtpIEQQPVI--GGRPVNLFRLYQLVQKLGGSRQVTQNNQWPRVAQKLGFppEQNPQVAQQLaqIYQRYLLP 87

                .
gi 30690195 131 F 131
Cdd:cd16871  88 Y 88

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30690195  76 GRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESYDSASA---KLIYVKYLDAFGR 133
Cdd:cd16866  28 GKELDLYLLYSKVTALGGWAKVTDKNKWEEILEDFNFPRGCSNAAfalKQIYLRYLEAYEK 88

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4B (ARID4B) and similar proteins; ARID4B, also called 180 kDa Sin3-associated polypeptide (p180), breast cancer-associated antigen BRCAA1, histone deacetylase complex subunit SAP180, or retinoblastoma-binding protein 1-like 1 (RBP1L1, or RBBP1L1), is a tumor suppressor involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. It associates with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with the breast cancer associated tumor suppressor ING1, the breast cancer metastasis suppressor BRMS1, and the ARID4 family homolog ARID4A ( also known as RBP1). ARID4B plays a causative role in metastatic progression of breast cancer. It may also be associated with regulating cell cycle. ARID4B contains a Tudor domain, a PWWP domain (also known as HATH domain or RBB1NT domain), an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a chromobarrel domain, and a C-terminal R2 domain.

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                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30690195  77 RTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESYDSASA---KLIYVKYLDAF 131
Cdd:cd16883  29 RNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGynvKCAYRKYLYGF 86

ARID/BRIGHT DNA binding domain of JARID proteins; The JARID subfamily within the JmjC protein family includes lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. The family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members of this subfamily contain the catalytic JmjC domain, JmjN, the AT-rich domain interacting domain (ARID)/BRIGHT domain, a C5HC2 zinc finger, as well as two or three plant homeodomain (PHD) fingers.

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                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30690195  75 EGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESYDSASAKLI--YVKYLDAF 131
Cdd:cd16864  28 ERKALDLFTLHKIVQEEGGFEEVTKERKWSKVARRLGYPPGKGVGSLLRghYERILYPY 86