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 1570334807  239 EEQSAFMKELENFFRERSME-FKHPKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFY 317
Cdd:smart00501   1 RERVLFLDRLYKFMEERGSPlKKIPVIGGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPDTSTSAASSLRKHY 80

                           90
                   ....*....|
gi 1570334807  318 EKALLDYERH 327
Cdd:smart00501  81 ERYLLPYERF 90

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 1570334807  239 EEQSAFMKELENFFRERSME-FKHPKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFY 317
Cdd:smart00501   1 RERVLFLDRLYKFMEERGSPlKKIPVIGGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPDTSTSAASSLRKHY 80

                           90
                   ....*....|
gi 1570334807  318 EKALLDYERH 327
Cdd:smart00501  81 ERYLLPYERF 90

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRERSM-EFKHPKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFYE 318
Cdd:cd16100     1 EREEFLEQLRAFLESRGTpLLKPPTIGGKPLDLYKLYRAVVSRGGYEKVTEKKLWKEVARKLGLPTSSTSAAQALKRIYE 80

                  ....*..
gi 1570334807 319 KALLDYE 325
Cdd:cd16100    81 KYLLPFE 87

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 448 VNVQKTKDCFEVYALVPGLLREEVRVQSDPaGRLVISGEPEHPNNPWGVT---------PFRKVVSLPSRIDPHQTSAVV 518
Cdd:COG0071     2 VDIEETDDAYVITADLPGVDKEDIDVTVEG-NVLTISGERKEEEEEEGENylrrerrygSFERSFTLPDDVDVDKIEASY 80

                          90
                  ....*....|.
gi 1570334807 519 TlHGQLFVRVP 529
Cdd:COG0071    81 E-NGVLTITLP 90

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 1570334807  239 EEQSAFMKELENFFRERSME-FKHPKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFY 317
Cdd:smart00501   1 RERVLFLDRLYKFMEERGSPlKKIPVIGGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPDTSTSAASSLRKHY 80

                           90
                   ....*....|
gi 1570334807  318 EKALLDYERH 327
Cdd:smart00501  81 ERYLLPYERF 90

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRERSM-EFKHPKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFYE 318
Cdd:cd16100     1 EREEFLEQLRAFLESRGTpLLKPPTIGGKPLDLYKLYRAVVSRGGYEKVTEKKLWKEVARKLGLPTSSTSAAQALKRIYE 80

                  ....*..
gi 1570334807 319 KALLDYE 325
Cdd:cd16100    81 KYLLPFE 87

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRERSMEFKH-PKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFYE 318
Cdd:cd16866     1 EYDAFLNELRQFHASRGTPFKKiPVVGGKELDLYLLYSKVTALGGWAKVTDKNKWEEILEDFNFPRGCSNAAFALKQIYL 80

                  ....*...
gi 1570334807 319 KALLDYER 326
Cdd:cd16866    81 RYLEAYEK 88

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID5A, ARID5B, and similar proteins; This subfamily contains ARID5A and its paralog ARID5B. ARID5A, also called modulator recognition factor 1 (MRF-1), is an estrogen receptor alpha (ER alpha)-interacting protein that is expressed abundantly in cardiovascular tissues and suppresses ER alpha-induced transactivation. It also plays an important role in the promotion of inflammatory processes and autoimmune diseases. ARID5B, also called MRF1-like protein or modulator recognition factor 2 (MRF-2), is a DNA-binding protein that directly interacts with plant homeodomain (PHD) finger 2 (PHF2) to form a protein kinase A (PKA)-dependent PHF2-ARID5B histone H3K9Me2 demethylase complex. It also functions as a transcriptional co-regulator for the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) and promotes chondrogenesis through histone modification. Moreover, ARID5B is highly expressed in the cardiovascular system and may play essential roles in the phenotypic change of smooth muscle cells (SMCs) through its regulation of SMC differentiation. Both ARID5A and ARID5B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRER--------SMEFKHpkfygegLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSW 311
Cdd:cd16869     1 EEQAFLKLLYKFMKDRgtpieripHLGFKQ-------IDLYTFFKLVQKLGGYEQVTAKRLWKHVYDELGGNPSSTSAAT 73

                          90
                  ....*....|....
gi 1570334807 312 TFRGFYEKALLDYE 325
Cdd:cd16869    74 CTRRHYEKLLLPYE 87

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5A (ARID5A) and similar proteins; ARID5A, also called modulator recognition factor 1 (MRF-1), is an estrogen receptor alpha (ER alpha)-interacting protein that is expressed abundantly in cardiovascular tissues and suppresses ER alpha-induced transactivation. It also associates with thyroid receptor alpha (TR alpha) and retinoid X receptor alpha (RXR alpha) in a ligand-dependent manner, and with ER beta, androgen receptor (AR), and the retinoic acid receptor (RAR) in a ligand-independent manner. ARID5A functions as a negative regulator of RORgamma-induced Th17 cell differentiation and may be involved in the pathogenesis of rheumatoid arthritis (RA). Moreover, it is an important transcriptional partner of the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) in stimulation of chondrocyte-specific transcription. Meanwhile, ARID5A plays an important role in promotion of inflammatory processes and autoimmune diseases. It works as a unique RNA binding protein, which stabilizes interleukin-6 (IL-6) but not tumor necrosis factor-alpha (TNF-alpha) mRNA through binding to the 3' untranslated region (UTR) of IL-6 mRNA, and inhibits the destabilizing effect of regnase-1 on IL-6 mRNA. ARID5A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRERSMEFKH-PKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFYE 318
Cdd:cd16884     1 EEQAFLVNLYKFMKERNTPIERiPHLGFKQINLWKIYKAVEKLGGYELVTARRLWKNVYDELGGSPGSTSAATCTRRHYE 80

                  ....*..
gi 1570334807 319 KALLDYE 325
Cdd:cd16884    81 RLVLPYV 87

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRERSMEF-KHPKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFYE 318
Cdd:cd16883     1 ERENFLQQLYKFMEDRGTPInKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYR 80

                  ....*....
gi 1570334807 319 KALLDYERH 327
Cdd:cd16883    81 KYLYGFEEY 89

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID4A, ARID4B and similar proteins; This subfamily contains ARID4A and its paralog ARID4B, both of which are retinoblastoma (Rb)-binding proteins that function as coactivators to enhance the androgen receptor (AR) and Rb transcriptional activity, and play important roles in the AR and Rb pathways to control male fertility. They also act as the leukemia and tumor suppressors involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. Moreover, they associate with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with each other, as well as with the breast cancer associated tumor suppressor ING1 and the breast cancer metastasis suppressor BRMS1. Both ARID4A and ARID4B contain 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRERSMEFKHPKFYG-EGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFYE 318
Cdd:cd16868     1 EKENFLEQLYKFMEDRGTPINKPPVLGyKDLDLFKLYKLVQELGGMERVSQGAKWRSIYQQLGIPVLNSAASHNIKQAYK 80

                  ....*..
gi 1570334807 319 KALLDYE 325
Cdd:cd16868    81 KYLYAFE 87

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3C (ARID3C) and similar proteins; ARID3C, also called Brightlike, is a new ARID3 family transcription factor that co-activates ARID3A-mediated immunoglobulin gene transcription. It also functions as a potential regulator of early events in B cell antigen receptor (BCR) signaling. ARID3C contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 234 ESGTEEEQSAFMKELENFFRERSMEFKH-PKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWT 312
Cdd:cd16880     9 ELDDDPKRKEFLDDLFSFMQKRGTPVNRiPIMAKQVLDLYTLYRLVTDKGGLVEVINKKIWREITKGLSLPTSITSAAFT 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1570334807 313 FRGFYEKALLDYE---RHKIKGGELNVPISS 340
Cdd:cd16880    89 LRTQYMKYLYPYEcekRALSSPGELQAAIDS 119

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4A (ARID4A) and similar proteins; ARID4A, also called retinoblastoma-binding protein 1 (RBBP1, or RBP1), is a leukemia and 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 ARID4B (also known as RBP1L1). ARID4A specifically interacts with retinoblastoma protein (pRb) and shows both HDAC-dependent and -independent repression activities. It is also involved in the pocket domain of pRb-mediated repression of E2F-dependent transcription and cellular proliferation. Moreover, it acts as a Runx2 coactivator and is involved in the regulation of osteoblastic differentiation in Runx2-osterix transcriptional cascade. ARID4A 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. The ARID and R2 domains are responsible for the repression activities. The Tudor, PWWP, and chromobarrel domains are all Royal Family domains, but only chromobarrel domain of ARID4A is responsible for recognizing both dsDNA and methylated histone tails, particularly H4K20me3, in chromatin remodeling and epigenetic regulation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 240 EQSAFMKELENFFRERSMEFKHPKFYG-EGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWTFRGFYE 318
Cdd:cd16882     1 ERDNFLQQLYKFMEDRGTPINKPPVLGyKDLNLFKLFRLVYQQGGCDNIESGSVWKQIYMDLGIPILNSAASYNVKTAYR 80

                  ....*..
gi 1570334807 319 KALLDYE 325
Cdd:cd16882    81 KYLYGFE 87

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3B (ARID3B) and similar proteins; ARID3B, also called Bright and dead ringer protein, or Bright-Dri-like protein (Bdp), is a DNA binding protein involved in cellular immortalization, epithelial-mesenchymal transition (EMT), and tumorigenesis. Its expression is differentially regulated in normal and malignant tissues. It is required for heart development by regulating the motility and differentiation of heart progenitors. ARID3B is overexpressed in neuroblastoma and ovarian cancer. It acts as a novel target with roles in cell motility in breast cancer cells, promotes migration of mouse embryo fibroblasts (MEFs) and breast cancer cells, and induces tumor necrosis factor alpha (TNFalpha)-mediated apoptosis. ARID3B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 234 ESGTEEEQSAFMKELENFFRERSMEFKH-PKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESFKPPKTCTTVSWT 312
Cdd:cd16879     8 ELDNDPKRKEFLDDLFAFMQKRGTPINRiPIMAKQVLDLYMLYKLVTEKGGLVEVINKKIWREITKGLNLPTSITSAAFT 87

                          90
                  ....*....|....*.
gi 1570334807 313 FRGFYEKALLDYERHK 328
Cdd:cd16879    88 LRTQYMKYLYPYECEK 103

ARID/BRIGHT DNA binding domain of dead ringer (Dri) from Drosophila melanogaster and similar proteins; Dri, also termed retained (retn), is a nuclear protein with a sequence-specific DNA-binding domain termed AT-rich DNA-interacting domain (ARID, also known as BRIGHT). It is a founding member of the ARID family. Sequence comparison shows that DRI belongs to the "extended" or e-ARID subfamily, which exhibits an extended region of similarity either side of the ARID. Dri plays an important role in embryogenesis. It functions as an essential transcription factor involved in aspects of dorsal/ventral and anterior/posterior axis patterning, as well as myogenesis and hindgut development.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 222 CFLDADHSYDGNESGTEEEqsaFMKELENFFRERSMEFKH-PKFYGEGLNCLKLWRAVTRLGGYDKVTSCKLWRQVGESF 300
Cdd:cd16881     4 FFEQFKQLYEISDDPKRKE---FLDDLFSFMQKRGTPVNRiPIMAKQVLDLYELYNLVVARGGLVEVINKKLWREITKGL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1570334807 301 KPPKTCTTVSWTFRGFYEKALLDYERHKIK 330
Cdd:cd16881    81 HLPSSITSAAFTLRTQYMKYLYPYECEKLK 110

Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570334807 444 DWvkvnvQKTKDCFEVYALVPGLLREEVRVQSDPAGRLVISG----EPEHPNNPWGVTP-----FRKVVSLPSRIDPHQT 514
Cdd:cd06472     3 DW-----KETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGerkkEEEKKGDDWHRVErssgrFVRRFRLPENADADEV 77

                          90
                  ....*....|....*
gi 1570334807 515 SAVVTlHGQLFVRVP 529
Cdd:cd06472    78 KAFLE-NGVLTVTVP 91