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 1831505860  263 AERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDlaESSAAGYQLRKH 342
Cdd:cd16865      1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIG--ASSSAAFTLRKN 78

                           90
                   ....*....|....*
gi 1831505860  343 YQRHLLMLECRETGR 357
Cdd:cd16865     79 YIKYLLAYECRFDRG 93

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  544 PAPSTTPAPQAASSSQAAPT---SGANTQPATPSASNQPPTPASAS--ASTTLHVEPASVAG-GSQAGSRAPSAGPGPSA 617
Cdd:PHA03247  2704 PPPTPEPAPHALVSATPLPPgpaAARQASPALPAAPAPPAVPAGPAtpGGPARPARPPTTAGpPAPAPPAAPAAGPPRRL 2783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  618 TPDSSTIPSASAAA------DAQTTTSSETSTPGEPTSSTPSDTPAPSTSVPPPTSVQPPQPQQPPQGPPGPPGPQQHPG 691
Cdd:PHA03247  2784 TRPAVASLSESRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  692 PYPGYPGYGPPGAMRPPAGFAPPPGAPYGYPPGAPPPAGFHPSHPQHPQHAQylawqqqryhqqQQHQQQQQQGAPGGPR 771
Cdd:PHA03247  2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP------------PPQPQPQPPPPPQPQP 2931

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831505860  772 PPYPYPGGPVPPGPPQNRMPPPPPAQGAPSPSGAAGSNGKQPRYGTPAPPSRASAPTPQPLSST 835
Cdd:PHA03247  2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

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 1831505860  263 AERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDlaESSAAGYQLRKH 342
Cdd:cd16865      1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIG--ASSSAAFTLRKN 78

                           90
                   ....*....|....*
gi 1831505860  343 YQRHLLMLECRETGR 357
Cdd:cd16865     79 YIKYLLAYECRFDRG 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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDlAESSAAGYQLRKHY 343
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYDKVTEKNLWREVAEKLGFP-PSAASAATQLKQIY 79

                   ....*...
gi 1831505860  344 QRHLLMLE 351
Cdd:pfam01388   80 EKYLLPYE 87

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  542 STPAPSTTPAPQAASSSQAAPTSGANTQPA--TPSASNQPPTPASASASTTLHVEPASVAggsqagSRAPSAGpGPSATP 619
Cdd:pfam17823   98 SEPATREGAADGAASRALAAAASSSPSSAAqsLPAAIAALPSEAFSAPRAAACRANASAA------PRAAIAA-ASAPHA 170

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1831505860  620 DSSTIPSASAAADAQTTTSSETSTPGEPTSSTPSD-TPAPSTS 661
Cdd:pfam17823  171 ASPAPRTAASSTTAASSTTAASSAPTTAASSAPATlTPARGIS 213

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  544 PAPSTTPAPQAASSSQAAPT---SGANTQPATPSASNQPPTPASAS--ASTTLHVEPASVAG-GSQAGSRAPSAGPGPSA 617
Cdd:PHA03247  2704 PPPTPEPAPHALVSATPLPPgpaAARQASPALPAAPAPPAVPAGPAtpGGPARPARPPTTAGpPAPAPPAAPAAGPPRRL 2783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  618 TPDSSTIPSASAAA------DAQTTTSSETSTPGEPTSSTPSDTPAPSTSVPPPTSVQPPQPQQPPQGPPGPPGPQQHPG 691
Cdd:PHA03247  2784 TRPAVASLSESRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  692 PYPGYPGYGPPGAMRPPAGFAPPPGAPYGYPPGAPPPAGFHPSHPQHPQHAQylawqqqryhqqQQHQQQQQQGAPGGPR 771
Cdd:PHA03247  2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP------------PPQPQPQPPPPPQPQP 2931

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831505860  772 PPYPYPGGPVPPGPPQNRMPPPPPAQGAPSPSGAAGSNGKQPRYGTPAPPSRASAPTPQPLSST 835
Cdd:PHA03247  2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  542 STPAPSTTPAPQAASSSQAAPTSGANTQPATPSASNQPPTPASASASTTLHVEPASVAGGSQAGSRAPSAGPGPSATPDS 621
Cdd:NF040712   193 GRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDE 272

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1831505860  622 STIPSASAAADAQTTTSSETSTPgEPTSSTPSDTPAPS 659
Cdd:NF040712   273 ATRDAGEPPAPGAAETPEAAEPP-APAPAAPAAPAAPE 309

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 1831505860  263 AERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDlaESSAAGYQLRKH 342
Cdd:cd16865      1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIG--ASSSAAFTLRKN 78

                           90
                   ....*....|....*
gi 1831505860  343 YQRHLLMLECRETGR 357
Cdd:cd16865     79 YIKYLLAYECRFDRG 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 1831505860   264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDLAESSaAGYQLRKHY 343
Cdd:smart01014    2 ERELFLDRLRKFMEKRGTPLDKIPVIGGKPLDLYRLYRAVQKRGGFDKVTKKKKWKQVARELGIPPSATS-AGTSLRKHY 80

                    ....*...
gi 1831505860   344 QRHLLMLE 351
Cdd:smart01014   81 EKYLLPYE 88

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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDLAESSAAgYQLRKHY 343
Cdd:cd16100      1 EREEFLEQLRAFLESRGTPLLKPPTIGGKPLDLYKLYRAVVSRGGYEKVTEKKLWKEVARKLGLPTSSTSAA-QALKRIY 79

                   ....*
gi 1831505860  344 QRHLL 348
Cdd:cd16100     80 EKYLL 84

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1A (ARID1A) and similar proteins; ARID1A, also called B120, BRG1-associated factor 250a (BAF250A), Osa homolog 1(OSA1), SWI-like protein, SWI/SNF complex protein p270, or SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 (SWI1), has been identified as a novel tumor suppressor in various tumor types. It interacts with BRG1 adenosine triphosphatase to form a SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complex, which plays a critical role in transcriptional control and gene expression. ARID1A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), and Eld/Osa homology domains (EHD) 1 and 2 within the C-terminus. The ARID in ARID1A binds nonspecific DNA in general and plays an important role in targeting SWI/SNF to chromatin. The EHD1 may be capable of mediating an intramolecular association with EHD2, and/or an intermolecular association resulting in homo- or hetero-dimerization. The EHD2 binds Swi2/Brahma homologue Brahma-related gene 1 (BRG1, also known as Snf2b), a human homologue of yeast Swi2.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANpdLAESSAAGYQLRKHY 343
Cdd:cd16876      2 ERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLN--VGTSSSAASSLKKQY 79

                           90
                   ....*....|
gi 1831505860  344 QRHLLMLECR 353
Cdd:cd16876     80 IQCLYAFECK 89

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  263 AERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWK------NLCTEANPDLAEssaag 336
Cdd:cd16871      1 AQPEQFMKSLREFMAKRGTPIEQQPVIGGRPVNLFRLYQLVQKLGGSRQVTQNNQWPrvaqklGFPPEQNPQVAQ----- 75

                           90
                   ....*....|....*
gi 1831505860  337 yQLRKHYQRHLLMLE 351
Cdd:cd16871     76 -QLAQIYQRYLLPYE 89

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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDLAESSAAgYQLRKHY 343
Cdd:cd16879     14 KRKEFLDDLFAFMQKRGTPINRIPIMAKQVLDLYMLYKLVTEKGGLVEVINKKIWREITKGLNLPTSITSAA-FTLRTQY 92

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1831505860  344 QRHLLMLECRETGRNPEDEVAFADKMKRQRKREP 377
Cdd:cd16879     93 MKYLYPYECEKKSLSSPAELQAAIDGNRREGRRP 126

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID3A, ARID3B, ARID3C, dead ringer (Dri) from Drosophila melanogaster, and similar proteins; The ARID3 subfamily includes AT-rich interactive domain (ARID, also known as BRIGHT)-containing proteins ARID3A, ARID3B and ARID3C, which are the most direct mammalian counterparts of the Drosophila "dead ringer" protein Dri. They consist of an acidic N-terminal region of unknown function, the central ARID matrix association (or attachment) region (MAR)-DNA binding domain, a SUMO-I conjugation (SUMO) motif, and a multifunctional homomerization/nuclear export REKLES domain in the C-terminal third of the molecule. The ARID domain in this subfamily has been described as the "extended" or e-ARID due to additional conserved sequences at both the N and C termini of the core ARID region. The REKLES domain is found only in the ARID3 subfamily. It has co-evolved with and regulates functional properties of the ARID DNA-binding domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  263 AERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDLAESSAAgYQLRKH 342
Cdd:cd16867     11 PKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYRLVVEKGGLVEVINKKIWREITKGLNLPSSITSAA-FTLRTQ 89

                           90       100
                   ....*....|....*....|
gi 1831505860  343 YQRHLLMLEC-RETGRNPED 361
Cdd:cd16867     90 YMKYLYPYECeKEKLSSPSE 109

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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEAN-PDLAesSAAGYQLRKH 342
Cdd:cd16868      1 EKENFLEQLYKFMEDRGTPINKPPVLGYKDLDLFKLYKLVQELGGMERVSQGAKWRSIYQQLGiPVLN--SAASHNIKQA 78

                   ....*....
gi 1831505860  343 YQRHLLMLE 351
Cdd:cd16868     79 YKKYLYAFE 87

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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDLAESSAAgYQLRKHY 343
Cdd:cd16881     19 KRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYNLVVARGGLVEVINKKLWREITKGLHLPSSITSAA-FTLRTQY 97

                           90       100
                   ....*....|....*....|...
gi 1831505860  344 QRHLLMLECRETGRNPEDEVAFA 366
Cdd:cd16881     98 MKYLYPYECEKLKLSTPAELQAA 120

DNA polymerase III subunit gamma/tau;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  545 APSTTPAPQAASSSQAAPTSGANTQPATPSASNQPPTPASASASTTLHVEPASVAGGSQAGSRAPSAGPGPSATPDSSti 624
Cdd:PRK12323   380 APVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA-- 457

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1831505860  625 PSASAAADAQTTTSSETSTPGEPTSSTPSDTPAPST 660
Cdd:PRK12323   458 PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPAD 493

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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEAN-PDLaeSSAAGYQLRKH 342
Cdd:cd16883      1 ERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGiPVL--NSAAGYNVKCA 78

                   ....*....
gi 1831505860  343 YQRHLLMLE 351
Cdd:cd16883     79 YRKYLYGFE 87

cytoskeleton protein RodZ;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  542 STPAPSTTPAPQAASSSQAAPTSGANTQ----PATPSASNQPPTPASASASTTLHVEPASVAgGSQAGSRAPSAGPGPSA 617
Cdd:PRK10856   168 TTTDPATTPAPAAPVDTTPTNSQTPAVAtapaPAVDPQQNAVVAPSQANVDTAATPAPAAPA-TPDGAAPLPTDQAGVST 246

                   ....*
gi 1831505860  618 TPDSS 622
Cdd:PRK10856   247 PAADP 251

DNA polymerase III subunit gamma/tau;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  544 PAPSTTPAPQAASSSQAAPTSGANTQPATPSASNQ------------PPTPASASASTTLHVEPASVAGGSQAGSRAPSA 611
Cdd:PRK07003   383 PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAaaatraeappaaPAPPATADRGDDAADGDAPVPAKANARASADSR 462

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1831505860  612 GPGPSATPDSSTIPSASAAADAQTTTSSETSTPGEPTSSTPSDTPAP 658
Cdd:PRK07003   463 CDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPD 509

DNA polymerase III subunits gamma and tau; Validated

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  545 APSTTPAPQAASSSQAAPTSGANTQPATPSASNQPPTPA--SASASTTLHVEPASVAGGSQAGSRAPSAGPGPSATPDSS 622
Cdd:PRK07764   596 GGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAapAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGG 675

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1831505860  623 TIPSASAAADAQTTTSSETSTPGEPTSSTPSDTPAPSTS 661
Cdd:PRK07764   676 AAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQA 714

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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANPDLAESSAAGYQlRKHY 343
Cdd:cd16885      1 DEQAFLVALYKYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGYETITARRQWKHIYDELGGNPGSTSAATCT-RRHY 79

                   ....*...
gi 1831505860  344 QRHLLMLE 351
Cdd:cd16885     80 ERLILPYE 87

Chitinase [Carbohydrate transport and metabolism];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  542 STPAPSTTPAPQAASSSQAAPTSGANTQPATPSASNQPPTPASASASTTLHVEPASVAGGSQAGSRAPSAGPGPSATPDS 621
Cdd:COG3469     78 TTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE 157

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1831505860  622 STIPSASAAADAQTTTSSETSTPGEPTSSTPSDTPAPSTSVPPPTS-V 668
Cdd:COG3469    158 TATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATtT 205

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 1831505860  264 ERRGFFERLIEFCEHNGEPLTMVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEAN-PDLaeSSAAGYQLRKH 342
Cdd:cd16882      1 ERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYQQGGCDNIESGSVWKQIYMDLGiPIL--NSAASYNVKTA 78

                   ....*....
gi 1831505860  343 YQRHLLMLE 351
Cdd:cd16882     79 YRKYLYGFE 87

ARID/BRIGHT DNA binding domain of lysine-specific demethylase KDM5C and KDM5D; This group includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C, also called histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, protein SmcX, or protein Xe169, 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, also called histocompatibility Y antigen (H-Y), histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or protein SmcY, 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. Both KDM5C and KDM5D contain 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 two plant homeodomain (PHD) fingers.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  268 FFERLIEFCEHNGEPLTmVPQVSKQSIDLHRLYIGVRAKGGFQQVTKDKYWKNLCTEANpdLAESSAAGYQLRKHYQRHL 347
Cdd:cd16875      7 YLDQIAKFWEIQGSSLK-IPNVERRILDLYSLSKIVQEEGGYEAICKDRRWARVAQRLG--YPPGKNIGSLLRSHYERII 83

                   ....*....
gi 1831505860  348 LMLECRETG 356
Cdd:cd16875     84 YPYEMYQSG 92

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831505860  544 PAPSTTPAPQAASSSQAAPT---SGANTQPATPSASNQPPTPASAS--ASTTLHVEPASVAG-GSQAGSRAPSAGPGPSA 617
Cdd:PHA03247  2704 PPPTPEPAPHALVSATPLPPgpaAARQASPALPAAPAPPAVPAGPAtpGGPARPARPPTTAGpPAPAPPAAPAAGPPRRL 2783