ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ARID1B and similar proteins; This subfamily contains ARID1A and its paralog ARID1B. They are mutually exclusive components of human SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complexes, but display different functions in development and cell-cycle control. SWI/SNF complexes containing ARID1A have an antiproliferative function, whereas the one harboring ARID1B shows a pro-proliferative function. ARID1A functions as an important tumor suppressor in various tumor types. It has been implicated in cell-cycle arrest, as well as in the interactions with p53 and BRG1/BRM and with topoisomerase II alpha. ARID1B may be considered as a potential therapeutic target for ARID1A-mutant cancers. Moreover, mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Mutations in the ARID1B gene also have been found in many cancers. Both ARID1A and ARID1B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1001 PDRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYTLRKHYT 1080
Cdd:cd16865    1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIGASSSAAFTLRKNYI 80

                         90
                 ....*....|...
gi 24647757 1081 KNLLTFECHFDRG 1093
Cdd:cd16865   81 KYLLAYECRFDRG 93

ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ARID1B and similar proteins; This subfamily contains ARID1A and its paralog ARID1B. They are mutually exclusive components of human SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complexes, but display different functions in development and cell-cycle control. SWI/SNF complexes containing ARID1A have an antiproliferative function, whereas the one harboring ARID1B shows a pro-proliferative function. ARID1A functions as an important tumor suppressor in various tumor types. It has been implicated in cell-cycle arrest, as well as in the interactions with p53 and BRG1/BRM and with topoisomerase II alpha. ARID1B may be considered as a potential therapeutic target for ARID1A-mutant cancers. Moreover, mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Mutations in the ARID1B gene also have been found in many cancers. Both ARID1A and ARID1B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1001 PDRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYTLRKHYT 1080
Cdd:cd16865    1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIGASSSAAFTLRKNYI 80

                         90
                 ....*....|...
gi 24647757 1081 KNLLTFECHFDRG 1093
Cdd:cd16865   81 KYLLAYECRFDRG 93

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757   1002 DRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGAS-SSAAYTLRKHYT 1080
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYDKVTEKNLWREVAEKLGFPPSaASAATQLKQIYE 80

                   ....*..
gi 24647757   1081 KNLLTFE 1087
Cdd:pfam01388   81 KYLLPYE 87

ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ARID1B and similar proteins; This subfamily contains ARID1A and its paralog ARID1B. They are mutually exclusive components of human SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complexes, but display different functions in development and cell-cycle control. SWI/SNF complexes containing ARID1A have an antiproliferative function, whereas the one harboring ARID1B shows a pro-proliferative function. ARID1A functions as an important tumor suppressor in various tumor types. It has been implicated in cell-cycle arrest, as well as in the interactions with p53 and BRG1/BRM and with topoisomerase II alpha. ARID1B may be considered as a potential therapeutic target for ARID1A-mutant cancers. Moreover, mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Mutations in the ARID1B gene also have been found in many cancers. Both ARID1A and ARID1B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1001 PDRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYTLRKHYT 1080
Cdd:cd16865    1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIGASSSAAFTLRKNYI 80

                         90
                 ....*....|...
gi 24647757 1081 KNLLTFECHFDRG 1093
Cdd:cd16865   81 KYLLAYECRFDRG 93

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) and similar proteins; ARID1B, also called BRG1-associated factor 250b (BAF250B), BRG1-binding protein ELD/OSA1, Osa homolog 2 (Osa2), or p250R, is the largest subunit of ATP-dependent SWItch/sucrose nonfermentable (SWI/SNF) chromatin remodeling complex, which plays a critical role in transcriptional control and gene expression. ARID1B exhibits tumour-suppressor activities in pancreatic cancer cell lines. Mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Moreover, mutations in the ARID1B gene have been found in many cancers. ARID1B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner similar to ARID1A.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1001 PDRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYTLRKHYT 1080
Cdd:cd16877    1 PERKLWVDRYLTFMEERGTPVASLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 80

                         90
                 ....*....|...
gi 24647757 1081 KNLLTFECHFDRG 1093
Cdd:cd16877   81 QYLFAFECKIERG 93

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757    1001 PDRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGI-GASSSAAYTLRKHY 1079
Cdd:smart01014    1 RERELFLDRLRKFMEKRGTPLDKIPVIGGKPLDLYRLYRAVQKRGGFDKVTKKKKWKQVARELGIpPSATSAGTSLRKHY 80

                    ....*...
gi 24647757    1080 TKNLLTFE 1087
Cdd:smart01014   81 EKYLLPYE 88

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757   1002 DRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGAS-SSAAYTLRKHYT 1080
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYDKVTEKNLWREVAEKLGFPPSaASAATQLKQIYE 80

                   ....*..
gi 24647757   1081 KNLLTFE 1087
Cdd:pfam01388   81 KYLLPYE 87

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 24647757 1002 DRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGAS-SSAAYTLRKHYT 1080
Cdd:cd16100    1 EREEFLEQLRAFLESRGTPLLKPPTIGGKPLDLYKLYRAVVSRGGYEKVTEKKLWKEVARKLGLPTSsTSAAQALKRIYE 80

                 ....*..
gi 24647757 1081 KNLLTFE 1087
Cdd:cd16100   81 KYLLPFE 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 24647757  993 KLYEMDDNPDRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGAS-SSA 1071
Cdd:cd16880    6 QLYELDDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYTLYRLVTDKGGLVEVINKKIWREITKGLSLPTSiTSA 85

                         90
                 ....*....|....*..
gi 24647757 1072 AYTLRKHYTKNLLTFEC 1088
Cdd:cd16880   86 AFTLRTQYMKYLYPYEC 102

ARID/BRIGHT DNA binding domain of Arabidopsis thaliana high mobility group B proteins HMGB9, HMGB10, HMGB11, HMGB15 and similar proteins; This subfamily includes a group of conserved plant DNA-binding proteins, including HMGB9 (or ARID-HMG1), HMGB10 (or ARID-HMG2), HMGB11, and HMGB15. They have been termed ARID-HMG proteins, due to containing two DNA-binding domains, an N-terminal AT-rich DNA-interacting domain (ARID, also known as BRIGHT), and a C-terminal high mobility group (HMG)-box domain. They are widely expressed in Arabidopsis and localize primarily to the nucleus. HMGB9/ARID-HMG1 binds specifically to A/T-rich DNA. HMGB15 is a transcription factor predominantly expressed in mature pollen grains and pollen tubes. It may work in the form of a homodimer, or interact with HMGB9, HMGB10 and HMGB11 to form heteromultimers in plant cells. HMGB15 is required for pollen tube growth in Arabidopsis and is involved in transcriptional regulation through the interaction with AGL66 and AGL104.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1002 DRRGWLDKLRAFMEERRTPITAcPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGAS-SSAAYTLRKHYT 1080
Cdd:cd16872    1 DPDLFWETLRKFHESLGTKFRI-PIVGGKELDLHRLYKEVTSRGGLEKVIKDRKWKEVAAVFNFPPTiTNASFVLRKYYL 79

                 ....*..
gi 24647757 1081 KNLLTFE 1087
Cdd:cd16872   80 SLLHHYE 86

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 24647757 1002 DRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGA-SSSAAYTLRKHYT 1080
Cdd:cd16868    1 EKENFLEQLYKFMEDRGTPINKPPVLGYKDLDLFKLYKLVQELGGMERVSQGAKWRSIYQQLGIPVlNSAASHNIKQAYK 80

                 ....*..
gi 24647757 1081 KNLLTFE 1087
Cdd:cd16868   81 KYLYAFE 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 24647757 1002 DRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGAS-SSAAYTLRKHYT 1080
Cdd:cd16866    1 EYDAFLNELRQFHASRGTPFKKIPVVGGKELDLYLLYSKVTALGGWAKVTDKNKWEEILEDFNFPRGcSNAAFALKQIYL 80

                 ....*..
gi 24647757 1081 KNLLTFE 1087
Cdd:cd16866   81 RYLEAYE 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 24647757 1002 DRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAA-YTLRKHYT 1080
Cdd:cd16883    1 ERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAgYNVKCAYR 80

                 ....*..
gi 24647757 1081 KNLLTFE 1087
Cdd:cd16883   81 KYLYGFE 87

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5B (ARID5B) and similar proteins; 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, which is a signal-sensing modulator of histone methylation and gene transcription. 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. Its polymorphism has been associated with risk for pediatric acute lymphoblastic leukemia (ALL). ARID5B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which can bind both the major and minor grooves of its target sequences.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1002 DRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIG-ASSSAAYTLRKHYT 1080
Cdd:cd16885    1 DEQAFLVALYKYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGYETITARRQWKHIYDELGGNpGSTSAATCTRRHYE 80

                         90
                 ....*....|....*.
gi 24647757 1081 KNLLTFEcHFDRGDID 1096
Cdd:cd16885   81 RLILPYE-RFIKGEED 95

ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5A (KDM5A); KDM5A, also called histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner; 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. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as three plant homeodomain (PHD) fingers.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1006 WLDKLRAFMEERRTPITaCPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYTLRKHYTKNLLT 1085
Cdd:cd16873    7 FLDQLAKFWELQGSTLK-IPVVERKILDLYALSKIVASEGGFEMVTKEKKWSKVGSRMGYLPGKGTGSLLKSHYERILYP 85

                 ..
gi 24647757 1086 FE 1087
Cdd:cd16873   86 YE 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757 1007 LDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYT-LRKHYTKNLLT 1085
Cdd:cd16870    9 LACIKKHLESQGINLTPPPLIGGCELDLPRLYHLVQELGGMQQVTDKKKWNKVADHLNIPKTAQDRPSkLQDAYCKYLLS 88

                 .
gi 24647757 1086 F 1086
Cdd:cd16870   89 Y 89

ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5B (KDM5B); KDM5B, also called cancer/testis antigen 31 (CT31), histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), is a member of the JARID subfamily within the JmjC proteins. It 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. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible earlygene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as three plant homeodomain (PHD) fingers.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647757 1006 WLDKLRAFMEERRTPITaCPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYTLRKHYTKNL 1083
Cdd:cd16874   10 FLDQIAKFWELQGCTLK-IPHVERKILDLFQLNKLVAEEGGFDLVCKERKWTKIATKMGFAPGKAVGSHIRAHYERIL 86

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757   662 YPPRPQYPP-GAYATGPPPPPTSqagaggANSMPSGAQAGGYPGRGMPNHTgqyPPYQWVPPSPqqtvpggAPGGAMVGN 740
Cdd:PHA03247 2573 PAPRPSEPAvTSRARRPDAPPQS------ARPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPP-------PPSPSPAAN 2636

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757   741 HVQGKGTPPPPVVGGPPPPQGSGSPRPlnylKQHLQHKGGYGGSPTPPQGPQgygngPTGMHPgmPMGPPHHMGPPHGPt 820
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDPAPGRVSR----PRRARRLGRAAQASSPPQRPR-----RRAARP--TVGSLTSLADPPPP- 2704

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757   821 nmgPPTSTPPqsqmlqggqpQGQGASGGPESGGPEHISQDNGISSSGPTGAAGMHAVTSVVTTGPDGTSMDEVSQQSTLS 900
Cdd:PHA03247 2705 ---PPTPEPA----------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP 2771

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647757   901 NASAASGEDPQCTTPKSRKNDPYSQSHLAPPSTSPHPVVMHPGGGPGEEYDMSSPPNWPRPAGSPQVfnhVPVPQEPFRS 980
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA---PPPPPGPPPP 2848

                  ....
gi 24647757   981 TITT 984
Cdd:PHA03247 2849 SLPL 2852