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Conserved domains on  [gi|767943247|ref|XP_011534290|]
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AT-rich interactive domain-containing protein 1B isoform X31 [Homo sapiens]

Protein Classification

ARID_ARID1B and BAF250_C domain-containing protein( domain architecture ID 13013841)

protein containing domains PHA03247, ARID_ARID1B, Med15, and BAF250_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAF250_C pfam12031
SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its ...
 1027-1282 5.81e-166

SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its homolog osa from fruit flies. They are part of the SWI/SNF-like ATP-dependent chromatin remodelling complex that regulates gene expression through regulating nucleosome remodelling. In humans there are two BAF250 isoforms, BAF250a/ARID1a and BAF250b/ARID1b. BAF250a/b may be E3 ubiquitin ligases that target histone H2B.


:

Pssm-ID: 463439  Cd Length: 257  Bit Score: 495.31  E-value: 5.81e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1027 SLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEV 1106
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRDEWWWDCLEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1107 LRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLI 1186
Cdd:pfam12031   81 LRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSAGPNSPLSPQRLVLEALCKLSVIDNNVDLI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1187 LATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDALAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNL 1266
Cdd:pfam12031  161 LATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDAEQNAQYVQSQHGL 240

                          250
                   ....*....|....*..
gi 767943247  1267 MHMQ-PPPLEPPSVDMM 1282
Cdd:pfam12031  241 NALRdNPELMGTSVDML 257
ARID_ARID1B cd16877
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) ...
 154-246 2.66e-65

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.


:

Pssm-ID: 350641  Cd Length: 93  Bit Score: 215.24  E-value: 2.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 233
Cdd:cd16877     1 PERKLWVDRYLTFMEERGTPVASLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 80

                          90
                  ....*....|...
gi 767943247  234 QYLFAFECKIERG 246
Cdd:cd16877    81 QYLFAFECKIERG 93
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 267-647 6.84e-12

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 70.04  E-value: 6.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   267 PPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPA---STPHGQMTPMQGGrsstiSVHDPFSDVSDSSFPKRNSMTP 343
Cdd:pfam09606  109 PMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRvgrMQPGGQAGGMMQP-----SSGQPGSGTPNQMGPNGGPGQG 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   344 NAPYQQGMSMPDVMGRMPYEPnkdpFGGMRKVPGSSEPFMTQ-----GQMPNSSMQDMYNQSPSGAMS----------NL 408
Cdd:pfam09606  184 QAGGMNGGQQGPMGGQMPPQM----GVPGMPGPADAGAQMGQqaqanGGMNPQQMGGAPNQVAMQQQQpqqqgqqsqlGM 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   409 GMGQRQQFPYGasyDRRHEPYGQQYPGQGPPSGQPPYGGHQPGlyPQQPNYKRHMDGMygPPAKRHEGdmyNMQYSSQQQ 488
Cdd:pfam09606  260 GINQMQQMPQG---VGGGAGQGGPGQPMGPPGQQPGAMPNVMS--IGDQNNYQQQQTR--QQQQQQGG---NHPAAHQQQ 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   489 EMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQThgiPPQMMGGPlqSSSSEGPQQNMWAARNDMPYPYQNRQGP 568
Cdd:pfam09606  330 MNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRG---QPGMMSSP--SPVPGQQVRQVTPNQFMRQSPQPSVPSP 404

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943247   569 GGPTQAPPYPGMNRtddmMVPDqrinhesqwPSHVSQRQPYMSSSASMQpiTRPPQPSYQTPPSLPNHISrAPSPASFQ 647
Cdd:pfam09606  405 QGPGSQPPQSHPGG----MIPS---------PALIPSPSPQMSQQPAQQ--RTIGQDSPGGSLNTPGQSA-VNSPLNPQ 467
 
Name Accession Description Interval E-value
BAF250_C pfam12031
SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its ...
 1027-1282 5.81e-166

SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its homolog osa from fruit flies. They are part of the SWI/SNF-like ATP-dependent chromatin remodelling complex that regulates gene expression through regulating nucleosome remodelling. In humans there are two BAF250 isoforms, BAF250a/ARID1a and BAF250b/ARID1b. BAF250a/b may be E3 ubiquitin ligases that target histone H2B.


Pssm-ID: 463439  Cd Length: 257  Bit Score: 495.31  E-value: 5.81e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1027 SLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEV 1106
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRDEWWWDCLEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1107 LRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLI 1186
Cdd:pfam12031   81 LRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSAGPNSPLSPQRLVLEALCKLSVIDNNVDLI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1187 LATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDALAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNL 1266
Cdd:pfam12031  161 LATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDAEQNAQYVQSQHGL 240

                          250
                   ....*....|....*..
gi 767943247  1267 MHMQ-PPPLEPPSVDMM 1282
Cdd:pfam12031  241 NALRdNPELMGTSVDML 257
ARID_ARID1B cd16877
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) ...
 154-246 2.66e-65

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.


Pssm-ID: 350641  Cd Length: 93  Bit Score: 215.24  E-value: 2.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 233
Cdd:cd16877     1 PERKLWVDRYLTFMEERGTPVASLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 80

                          90
                  ....*....|...
gi 767943247  234 QYLFAFECKIERG 246
Cdd:cd16877    81 QYLFAFECKIERG 93
BRIGHT smart00501
BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a ...
 154-245 1.69e-31

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


Pssm-ID: 128777 [Multi-domain]  Cd Length: 93  Bit Score: 118.53  E-value: 1.69e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247    154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVG-TSSSAASSLKKQY 232
Cdd:smart00501    1 RERVLFLDRLYKFMEERGSPLKKIPVIGGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPdTSTSAASSLRKHY 80

                            90
                    ....*....|...
gi 767943247    233 IQYLFAFECKIER 245
Cdd:smart00501   81 ERYLLPYERFLRG 93
ARID pfam01388
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ...
 155-240 6.14e-25

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


Pssm-ID: 460187  Cd Length: 87  Bit Score: 99.62  E-value: 6.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   155 ERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVG-TSSSAASSLKKQYI 233
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYDKVTEKNLWREVAEKLGFPpSAASAATQLKQIYE 80


                   ....*..
gi 767943247   234 QYLFAFE 240
Cdd:pfam01388   81 KYLLPYE 87
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 267-647 6.84e-12

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 70.04  E-value: 6.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   267 PPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPA---STPHGQMTPMQGGrsstiSVHDPFSDVSDSSFPKRNSMTP 343
Cdd:pfam09606  109 PMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRvgrMQPGGQAGGMMQP-----SSGQPGSGTPNQMGPNGGPGQG 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   344 NAPYQQGMSMPDVMGRMPYEPnkdpFGGMRKVPGSSEPFMTQ-----GQMPNSSMQDMYNQSPSGAMS----------NL 408
Cdd:pfam09606  184 QAGGMNGGQQGPMGGQMPPQM----GVPGMPGPADAGAQMGQqaqanGGMNPQQMGGAPNQVAMQQQQpqqqgqqsqlGM 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   409 GMGQRQQFPYGasyDRRHEPYGQQYPGQGPPSGQPPYGGHQPGlyPQQPNYKRHMDGMygPPAKRHEGdmyNMQYSSQQQ 488
Cdd:pfam09606  260 GINQMQQMPQG---VGGGAGQGGPGQPMGPPGQQPGAMPNVMS--IGDQNNYQQQQTR--QQQQQQGG---NHPAAHQQQ 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   489 EMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQThgiPPQMMGGPlqSSSSEGPQQNMWAARNDMPYPYQNRQGP 568
Cdd:pfam09606  330 MNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRG---QPGMMSSP--SPVPGQQVRQVTPNQFMRQSPQPSVPSP 404

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943247   569 GGPTQAPPYPGMNRtddmMVPDqrinhesqwPSHVSQRQPYMSSSASMQpiTRPPQPSYQTPPSLPNHISrAPSPASFQ 647
Cdd:pfam09606  405 QGPGSQPPQSHPGG----MIPS---------PALIPSPSPQMSQQPAQQ--RTIGQDSPGGSLNTPGQSA-VNSPLNPQ 467
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 423-576 2.54e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.10  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   423 DRRHEPYGQQYPGQGPPSGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGdmynmqyssQQQEMYNQYGGsysgpd 502
Cdd:TIGR01628  365 EQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPR---------MSMMPTPMGPG------ 429

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943247   503 rRPIQGQYPYPYSRERMQGPGQIQTHGIPPQMmggPLQSSSSEGPQQNMWAARNDMPYPYQNRQGPGGPTQ---APP 576
Cdd:TIGR01628  430 -GPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQ---PVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVlasATP 502
PHA03377 PHA03377
EBNA-3C; Provisional
 256-680 8.28e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.81  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  256 TGDTKKQPKLQPPSPANSG---SLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQGGRSSTisvhDPFSDVSD 332
Cdd:PHA03377  543 SGRRQKRATPPKVSPSDRGppkASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPAS----GPHEKQPP 618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  333 SSFPKRNSMTPNAPYQQGMSMPDVMGRMP---YEPNKDPFG-GMRKVPGSSEPFMTQGQMPNSS---------MQDMYNQ 399
Cdd:PHA03377  619 SSAPRDMAPSVVRMFLRERLLEQSTGPKPksfWEMRAGRDGsGIQQEPSSRRQPATQSTPPRPSwlpsvfvlpSVDAGRA 698

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  400 SPSGAMSNLGMGQRQqfPYGASYDRRHEPYG-----QQYPGQGP-PSGQPPYGGHQPGLYPQQPnYKRHMDGMygPPAKR 473
Cdd:PHA03377  699 QPSEESHLSSMSPTQ--PISHEEQPRYEDPDdpldlSLHPDQAPpPSHQAPYSGHEEPQAQQAP-YPGYWEPR--PPQAP 773

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  474 HEGdmynMQYSSQQQEMYNQYGGsYSGPdrRPIQGQYP------YPYSRERMQGPGQiqthgippqmmgGPlqssssegp 547
Cdd:PHA03377  774 YLG----YQEPQAQGVQVSSYPG-YAGP--WGLRAQHPryrhswAYWSQYPGHGHPQ------------GP--------- 825

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  548 qqnmWAARNdmPYPyqnrqgpggPTQAPPYPGMNRTddmmvpdqrinhesqwpsHVSQRQPymsssasMQPITRPPQPSY 627
Cdd:PHA03377  826 ----WAPRP--PHL---------PPQWDGSAGHGQD------------------QVSQFPH-------LQSETGPPRLQL 865

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767943247  628 QTPPSLPNHI----SRAPSPASFQRSLENRMSPSKSPfLPSMKMQKVMPTVPTSQVT 680
Cdd:PHA03377  866 SQVPQLPYSQtlvsSSAPSWSSPQPRAPIRPIPTRFP-PPPMPLQDSMAVGCDSSGT 921
 
Name Accession Description Interval E-value
BAF250_C pfam12031
SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its ...
 1027-1282 5.81e-166

SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its homolog osa from fruit flies. They are part of the SWI/SNF-like ATP-dependent chromatin remodelling complex that regulates gene expression through regulating nucleosome remodelling. In humans there are two BAF250 isoforms, BAF250a/ARID1a and BAF250b/ARID1b. BAF250a/b may be E3 ubiquitin ligases that target histone H2B.


Pssm-ID: 463439  Cd Length: 257  Bit Score: 495.31  E-value: 5.81e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1027 SLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEV 1106
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRDEWWWDCLEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1107 LRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLI 1186
Cdd:pfam12031   81 LRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSAGPNSPLSPQRLVLEALCKLSVIDNNVDLI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  1187 LATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDALAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNL 1266
Cdd:pfam12031  161 LATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDAEQNAQYVQSQHGL 240

                          250
                   ....*....|....*..
gi 767943247  1267 MHMQ-PPPLEPPSVDMM 1282
Cdd:pfam12031  241 NALRdNPELMGTSVDML 257
ARID_ARID1B cd16877
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) ...
 154-246 2.66e-65

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.


Pssm-ID: 350641  Cd Length: 93  Bit Score: 215.24  E-value: 2.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 233
Cdd:cd16877     1 PERKLWVDRYLTFMEERGTPVASLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 80

                          90
                  ....*....|...
gi 767943247  234 QYLFAFECKIERG 246
Cdd:cd16877    81 QYLFAFECKIERG 93
ARID_ARID1A cd16876
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1A (ARID1A) ...
 154-246 1.56e-48

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.


Pssm-ID: 350640  Cd Length: 93  Bit Score: 167.53  E-value: 1.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 233
Cdd:cd16876     1 PERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 80

                          90
                  ....*....|...
gi 767943247  234 QYLFAFECKIERG 246
Cdd:cd16876    81 QCLYAFECKIERG 93
ARID_ARID1A-like cd16865
ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ...
 154-246 9.30e-48

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.


Pssm-ID: 350629  Cd Length: 93  Bit Score: 165.14  E-value: 9.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYI 233
Cdd:cd16865     1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAEVTKNKKWKEICTELNIGASSSAAFTLRKNYI 80

                          90
                  ....*....|...
gi 767943247  234 QYLFAFECKIERG 246
Cdd:cd16865    81 KYLLAYECRFDRG 93
BRIGHT smart00501
BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a ...
 154-245 1.69e-31

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


Pssm-ID: 128777 [Multi-domain]  Cd Length: 93  Bit Score: 118.53  E-value: 1.69e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247    154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVG-TSSSAASSLKKQY 232
Cdd:smart00501    1 RERVLFLDRLYKFMEERGSPLKKIPVIGGKPLDLYRLYRLVQERGGYDQVTKDKKWKEIARELGIPdTSTSAASSLRKHY 80

                            90
                    ....*....|...
gi 767943247    233 IQYLFAFECKIER 245
Cdd:smart00501   81 ERYLLPYERFLRG 93
ARID smart01014
ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction ...
 154-240 1.92e-26

ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction domain) family of DNA-binding proteins are found in fungi and invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative transcriptional regulation and a likely involvement in the modification of chromatin structure. The basic structure of the ARID domain domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes: Minimal ARID proteins that consist of a core domain formed by six alpha helices; ARID proteins that supplement the core domain with an N-terminal alpha-helix; and Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini.


Pssm-ID: 198082 [Multi-domain]  Cd Length: 88  Bit Score: 104.24  E-value: 1.92e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247    154 PERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNV-GTSSSAASSLKKQY 232
Cdd:smart01014    1 RERELFLDRLRKFMEKRGTPLDKIPVIGGKPLDLYRLYRAVQKRGGFDKVTKKKKWKQVARELGIpPSATSAGTSLRKHY 80


                    ....*...
gi 767943247    233 IQYLFAFE 240
Cdd:smart01014   81 EKYLLPYE 88
ARID pfam01388
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ...
 155-240 6.14e-25

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


Pssm-ID: 460187  Cd Length: 87  Bit Score: 99.62  E-value: 6.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   155 ERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVG-TSSSAASSLKKQYI 233
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYDKVTEKNLWREVAEKLGFPpSAASAATQLKQIYE 80


                   ....*..
gi 767943247   234 QYLFAFE 240
Cdd:pfam01388   81 KYLLPYE 87
ARID_ARID3 cd16867
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID3A, ...
 146-249 8.09e-25

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.


Pssm-ID: 350631  Cd Length: 118  Bit Score: 100.64  E-value: 8.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  146 KVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAA 225
Cdd:cd16867     3 QLYELSDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYRLVVEKGGLVEVINKKIWREITKGLNLPSSITSA 82

                          90       100
                  ....*....|....*....|....*
gi 767943247  226 S-SLKKQYIQYLFAFECKIERGEEP 249
Cdd:cd16867    83 AfTLRTQYMKYLYPYECEKEKLSSP 107
ARID_ARID3A cd16878
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3A (ARID3A) ...
 142-262 4.63e-23

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3A (ARID3A) and similar proteins; ARID3A, also called B-cell regulator of IgH transcription (Bright), dead ringer-like protein 1 (Dril1), or E2F-binding protein 1 (E2FBP1), is an ubiquitously expressed DNA-binding protein that has been implicated in embryonic patterning, cell lineage gene regulation, and cell cycle control, chromatin remodeling and transcriptional regulation. It was originally identified as a B cell-specific trans-activator of immunoglobulin heavy-chain (IgH) transcription, which increases immunoglobulin transcription in antigen-activated B cells and plays regulatory roles in hematopoiesis. It also functions as an E2F transcription regulator, inducing promyelocytic leukemia protein (PML) reduction and suppressing the formation of PML-nuclear bodies. It antagonizes the p16(INK4A)-Rb tumor suppressor machinery by regulating PML stability. ARID3A transcriptional activity can be modulated by SUMO (Small Ubiquitin-related Modifier) modification through the interaction with the SUMO-conjugating enzyme Ubc9. ARID3A also plays an important role in marginal zone B lymphocyte development and autoantibody production. Furthermore, ARID3A is a direct p53 target gene. It controls cell growth in a p53-dependent manner. ARID3A 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.


Pssm-ID: 350642  Cd Length: 133  Bit Score: 96.28  E-value: 4.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  142 EKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTS 221
Cdd:cd16878     9 EQFKQLYELDGDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYMLYVLVTEKGGLVEVINKKLWREITKGLNLPTS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767943247  222 SSAAS-SLKKQYIQYLFAFECKiERGEEPPPEVFSTGDTKKQ 262
Cdd:cd16878    89 ITSAAfTLRTQYMKYLYPYECE-KRGLSNPNELQAAIDSNRR 129
ARID_ARID3B cd16879
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3B (ARID3B) ...
 146-267 8.41e-23

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.


Pssm-ID: 350643  Cd Length: 126  Bit Score: 95.08  E-value: 8.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  146 KVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAA 225
Cdd:cd16879     5 KLYELDNDPKRKEFLDDLFAFMQKRGTPINRIPIMAKQVLDLYMLYKLVTEKGGLVEVINKKIWREITKGLNLPTSITSA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767943247  226 S-SLKKQYIQYLFAFECKiERGEEPPPEVFSTGDTKKQPKLQP 267
Cdd:cd16879    85 AfTLRTQYMKYLYPYECE-KKSLSSPAELQAAIDGNRREGRRP 126
ARID cd16100
ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of ...
 155-240 8.65e-22

ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of transcription factors, found in a broad array of organisms from fungi to mammals, is characterized by a highly conserved, helix-turn-helix DNA binding domain that binds to the major groove of DNA. The ARID domain, also called BRIGHT, was first identified in the mouse B-cell-specific transcription factor Bright and in the product of the dead ringer (dri) gene of Drosophila melanogaster. ARID family members are implicated in normal development, differentiation, cell cycle regulation, transcriptional activation and chromatin remodeling. Different family members exhibit different DNA-binding properties. Drosophila Dri, mammalian ARID3A/3B/3C and ARID5A/5B, selectively bind AT-rich sites. However, ARID1A/1B, Drosophila Osa, yeast SWI1, ARID2, ARID4A/4B, JARID1A/1B/1C/1D, and JARID2, bind DNA without sequence specificity.


Pssm-ID: 350627  Cd Length: 87  Bit Score: 90.88  E-value: 8.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  155 ERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAA-SSLKKQYI 233
Cdd:cd16100     1 EREEFLEQLRAFLESRGTPLLKPPTIGGKPLDLYKLYRAVVSRGGYEKVTEKKLWKEVARKLGLPTSSTSAaQALKRIYE 80


                  ....*..
gi 767943247  234 QYLFAFE 240
Cdd:cd16100    81 KYLLPFE 87
ARID_ARID3C cd16880
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3C (ARID3C) ...
 142-262 1.34e-21

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.


Pssm-ID: 350644  Cd Length: 127  Bit Score: 91.63  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  142 EKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTS 221
Cdd:cd16880     2 EQFKQLYELDDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYTLYRLVTDKGGLVEVINKKIWREITKGLSLPTS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767943247  222 SSAAS-SLKKQYIQYLFAFECKiERGEEPPPEVFSTGDTKKQ 262
Cdd:cd16880    82 ITSAAfTLRTQYMKYLYPYECE-KRALSSPGELQAAIDSNRR 122
ARID_Dri-like cd16881
ARID/BRIGHT DNA binding domain of dead ringer (Dri) from Drosophila melanogaster and similar ...
 142-249 1.37e-19

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.


Pssm-ID: 350645  Cd Length: 125  Bit Score: 86.10  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  142 EKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNV-GT 220
Cdd:cd16881     6 EQFKQLYEISDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYNLVVARGGLVEVINKKLWREITKGLHLpSS 85

                          90       100
                  ....*....|....*....|....*....
gi 767943247  221 SSSAASSLKKQYIQYLFAFECKIERGEEP 249
Cdd:cd16881    86 ITSAAFTLRTQYMKYLYPYECEKLKLSTP 114
ARID_ARID4 cd16868
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID4A, ...
 155-240 9.72e-17

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.


Pssm-ID: 350632  Cd Length: 87  Bit Score: 76.27  E-value: 9.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  155 ERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAAS-SLKKQYI 233
Cdd:cd16868     1 EKENFLEQLYKFMEDRGTPINKPPVLGYKDLDLFKLYKLVQELGGMERVSQGAKWRSIYQQLGIPVLNSAAShNIKQAYK 80


                  ....*..
gi 767943247  234 QYLFAFE 240
Cdd:cd16868    81 KYLYAFE 87
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 267-647 6.84e-12

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 70.04  E-value: 6.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   267 PPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPA---STPHGQMTPMQGGrsstiSVHDPFSDVSDSSFPKRNSMTP 343
Cdd:pfam09606  109 PMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRvgrMQPGGQAGGMMQP-----SSGQPGSGTPNQMGPNGGPGQG 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   344 NAPYQQGMSMPDVMGRMPYEPnkdpFGGMRKVPGSSEPFMTQ-----GQMPNSSMQDMYNQSPSGAMS----------NL 408
Cdd:pfam09606  184 QAGGMNGGQQGPMGGQMPPQM----GVPGMPGPADAGAQMGQqaqanGGMNPQQMGGAPNQVAMQQQQpqqqgqqsqlGM 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   409 GMGQRQQFPYGasyDRRHEPYGQQYPGQGPPSGQPPYGGHQPGlyPQQPNYKRHMDGMygPPAKRHEGdmyNMQYSSQQQ 488
Cdd:pfam09606  260 GINQMQQMPQG---VGGGAGQGGPGQPMGPPGQQPGAMPNVMS--IGDQNNYQQQQTR--QQQQQQGG---NHPAAHQQQ 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   489 EMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQThgiPPQMMGGPlqSSSSEGPQQNMWAARNDMPYPYQNRQGP 568
Cdd:pfam09606  330 MNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRG---QPGMMSSP--SPVPGQQVRQVTPNQFMRQSPQPSVPSP 404

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943247   569 GGPTQAPPYPGMNRtddmMVPDqrinhesqwPSHVSQRQPYMSSSASMQpiTRPPQPSYQTPPSLPNHISrAPSPASFQ 647
Cdd:pfam09606  405 QGPGSQPPQSHPGG----MIPS---------PALIPSPSPQMSQQPAQQ--RTIGQDSPGGSLNTPGQSA-VNSPLNPQ 467
ARID_ARID2 cd16866
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and ...
 163-240 1.68e-11

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and similar proteins; ARID2, also called BRG1-associated factor 200 (BAF200) or zinc finger protein with activation potential (Zipzap/p200), is a novel serum response factor (SRF)-binding protein with multiple conserved domains, including an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), RFX DNA-binding domain, a glutamine-rich domain, and two C2H2 zinc fingers. It binds DNA without sequence specificity. ARID2 is an intrinsic subunit of PBAF (SWI/SNF-B) remodeling complex, which needs ARID2 to play an essential role in promoting osteoblast differentiation, maintaining cellular identity and activating tissue-specific gene expression. Moreover, ARID2 may function as a tumor suppressor in many cancers. It may also serve as a transcription co-activator for the regulation of cardiac gene expression, and is required for heart morphogenesis and coronary artery development.


Pssm-ID: 350630  Cd Length: 88  Bit Score: 61.51  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  163 YLTFMEE-------RGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNV-GTSSSAASSLKKQYIQ 234
Cdd:cd16866     2 YDAFLNElrqfhasRGTPFKKIPVVGGKELDLYLLYSKVTALGGWAKVTDKNKWEEILEDFNFpRGCSNAAFALKQIYLR 81


                  ....*.
gi 767943247  235 YLFAFE 240
Cdd:cd16866    82 YLEAYE 87
ARID_HMGB9-like cd16872
ARID/BRIGHT DNA binding domain of Arabidopsis thaliana high mobility group B proteins HMGB9, ...
 155-240 1.90e-11

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.


Pssm-ID: 350636  Cd Length: 86  Bit Score: 61.51  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  155 ERKLWVDRYLTFMEERGSPvSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVG-TSSSAASSLKKQYI 233
Cdd:cd16872     1 DPDLFWETLRKFHESLGTK-FRIPIVGGKELDLHRLYKEVTSRGGLEKVIKDRKWKEVAAVFNFPpTITNASFVLRKYYL 79


                  ....*..
gi 767943247  234 QYLFAFE 240
Cdd:cd16872    80 SLLHHYE 86
ARID_Swi1p-like cd16871
ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and ...
 166-240 4.45e-11

ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and similar proteins; Saccharomyces cerevisiae Swi1p, also called SWI/SNF chromatin-remodeling complex subunit SWI1, regulatory protein GAM3, or transcription regulatory protein ADR6, is a transcription regulatory protein that is a subunit of the SWI/SNF complex, which plays critical roles in the regulation of gene transcription and expression. It can exist as a prion, [SWI(+)], which demonstrates a link between prionogenesis and global transcriptional regulation. Swi1p contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT) that binds DNA nonspecifically. This subfamily also includes Schizosaccharomyces pombe SWI/SNF chromatin-remodeling complex subunit sol1 (sol1p, also known as switch one-like protein). sol1p is a homolog of S. cerevisiae Swi1p and is also a part of SWI/SNF chromatin-remodeling complex.


Pssm-ID: 350635  Cd Length: 90  Bit Score: 60.34  E-value: 4.45e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943247  166 FMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSA--ASSLKKQYIQYLFAFE 240
Cdd:cd16871    13 FMAKRGTPIEQQPVIGGRPVNLFRLYQLVQKLGGSRQVTQNNQWPRVAQKLGFPPEQNPqvAQQLAQIYQRYLLPYE 89
ARID_ARID4B cd16883
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4B (ARID4B) ...
 155-240 6.65e-10

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.


Pssm-ID: 350647  Cd Length: 92  Bit Score: 57.29  E-value: 6.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  155 ERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAAS-SLKKQYI 233
Cdd:cd16883     1 ERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGyNVKCAYR 80


                  ....*..
gi 767943247  234 QYLFAFE 240
Cdd:cd16883    81 KYLYGFE 87
ARID_JARID cd16864
ARID/BRIGHT DNA binding domain of JARID proteins; The JARID subfamily within the JmjC protein ...
 166-240 3.24e-09

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.


Pssm-ID: 350628  Cd Length: 87  Bit Score: 55.01  E-value: 3.24e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943247  166 FMEERGSPVSsLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFE 240
Cdd:cd16864    14 FWELQGSSLK-IPNVERKALDLFTLHKIVQEEGGFEEVTKERKWSKVARRLGYPPGKGVGSLLRGHYERILYPYD 87
ARID_ARID5 cd16869
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID5A, ...
 166-212 1.46e-08

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).


Pssm-ID: 350633  Cd Length: 87  Bit Score: 53.07  E-value: 1.46e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767943247  166 FMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWREL 212
Cdd:cd16869    12 FMKDRGTPIERIPHLGFKQIDLYTFFKLVQKLGGYEQVTAKRLWKHV 58
ARID_ARID4A cd16882
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4A (ARID4A) ...
 155-240 3.02e-08

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.


Pssm-ID: 350646  Cd Length: 87  Bit Score: 52.28  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  155 ERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGT-SSSAASSLKKQYI 233
Cdd:cd16882     1 ERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYQQGGCDNIESGSVWKQIYMDLGIPIlNSAASYNVKTAYR 80


                  ....*..
gi 767943247  234 QYLFAFE 240
Cdd:cd16882    81 KYLYGFE 87
ARID_ARID5A cd16884
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5A (ARID5A) ...
 155-216 1.01e-05

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).


Pssm-ID: 350648  Cd Length: 87  Bit Score: 44.99  E-value: 1.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943247  155 ERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNL 216
Cdd:cd16884     1 EEQAFLVNLYKFMKERNTPIERIPHLGFKQINLWKIYKAVEKLGGYELVTARRLWKNVYDEL 62
ARID_JARD2 cd16870
ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and ...
 167-239 1.58e-05

ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and similar proteins; JARID2, also called protein Jumonji, is a DNA-binding protein that contains both the Jumonji C (JmjC) domain and AT-rich DNA-interacting domain (ARID, also known as BRIGHT). It is an interacting component of Polycomb repressive complex-2 (PRC2) that catalyzes methylation of lysine 27 of histone H3 (H3K27) and regulates important gene expression patterns during development. It exhibits nucleosome-binding activity that contributes to PRC2 stimulation. However, unlike other JmjC domain-containing proteins, JARID2 is catalytically inactive due to the lack of conserved residues essential for histone demethylase activity. JARID2 is also involved in transforming growth factor-beta (TGF-beta)-induced epithelial-mesenchymal transition (EMT) of lung and colon cancer cell lines through the modulation of histone H3K27 methylation. Moreover, JARID2 is a part of GLP- and G9a-containing protein complex that promotes lysine 9 on histone H3 (H3K9) methylation on the cyclin D1 promoter and silences the expression of cyclin D1 and other cell cycle genes. It functions as a transcriptional repressor that plays critical roles in embryonic development including heart development in mice, and regulates cardiomyocyte proliferation via interaction with retinoblastoma protein (Rb), one of the master regulatory genes of the cell cycle. Furthermore, JARID2 acts as a transcriptional repressor of target genes, including Notch1. It directly binds to SETDB1 (SET domain, bifurcated 1) to form a complex that plays an important role in a novel process involving the modification of H3K9 methylation during heart development. Meanwhile, JARID2 is a key transcriptional repressor that plays a role in invariant natural killer T (iNKT) cell maturation. It regulates promyelocytic leukemia zinc finger (PLZF) expression by linking T-cell receptor (TCR) signaling to H3K9me3. JARID2 polymorphisms are associated with non-syndromic orofacial clefts (NSOC) susceptibility.


Pssm-ID: 350634  Cd Length: 112  Bit Score: 45.29  E-value: 1.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943247  167 MEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNV-GTSSSAASSLKKQYIQYLFAF 239
Cdd:cd16870    16 LESQGINLTPPPLIGGCELDLPRLYHLVQELGGMQQVTDKKKWNKVADHLNIpKTAQDRPSKLQDAYCKYLLSY 89
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 262-608 2.14e-05

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 49.18  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   262 QPKLQPPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQGGRSStisvHDPFSDVSDSSFPKRNSM 341
Cdd:pfam03157  279 QQGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQ----QGQQPAQGQQPGQGQPGY 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   342 TPNAPYQQGMSMPDVMGRMPYEPNKDPF-----GGMRKVPGSSEPFMTQGQMPNSSMQDMYNQSPSGA---------MSN 407
Cdd:pfam03157  355 YPTSPQQPGQGQPGYYPTSQQQPQQGQQpeqgqQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSgqgqpgyypTSP 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   408 LGMGQRQQFPYGASYDRRHEPYGQQyPGQGPPSGQPPYGGH-------QPGLYPQQPNYKRHMDgmyGPPAKRHEGDMYN 480
Cdd:pfam03157  435 QQSGQGQQPGQGQQPGQEQPGQGQQ-PGQGQQGQQPGQPEQgqqpgqgQPGYYPTSPQQSGQGQ---QLGQWQQQGQGQP 510

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   481 MQYSSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQTHGIPPQMMGGPLQSSSSEGPQQNMWAARNDMP- 559
Cdd:pfam03157  511 GYYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPg 590

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767943247   560 ------YPYQNRQ-GPGGPTQAPPYPGMNRTDDMMVPDQRINHESQWPSHVSQRQP 608
Cdd:pfam03157  591 qgqpgyYPTSPQQsGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQGYYPTSPQQP 646
ARID_KDM5A cd16873
ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5A (KDM5A); KDM5A, also called ...
 159-240 4.53e-05

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.


Pssm-ID: 350637  Cd Length: 92  Bit Score: 43.33  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  159 WVDRYLTFMEERGSPVSsLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFA 238
Cdd:cd16873     7 FLDQLAKFWELQGSTLK-IPVVERKILDLYALSKIVASEGGFEMVTKEKKWSKVGSRMGYLPGKGTGSLLKSHYERILYP 85


                  ..
gi 767943247  239 FE 240
Cdd:cd16873    86 YE 87
ARID_KDM5C_5D cd16875
ARID/BRIGHT DNA binding domain of lysine-specific demethylase KDM5C and KDM5D; This group ...
 159-240 4.80e-05

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.


Pssm-ID: 350639  Cd Length: 92  Bit Score: 43.37  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  159 WVDRYLTFMEERGSPVSsLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFA 238
Cdd:cd16875     7 YLDQIAKFWEIQGSSLK-IPNVERRILDLYSLSKIVQEEGGYEAICKDRRWARVAQRLGYPPGKNIGSLLRSHYERIIYP 85


                  ..
gi 767943247  239 FE 240
Cdd:cd16875    86 YE 87
ARID_KDM5B cd16874
ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5B (KDM5B); KDM5B, also called ...
 159-239 1.65e-04

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.


Pssm-ID: 350638  Cd Length: 90  Bit Score: 41.85  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  159 WVDRYLTFMEERGSPVSsLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFA 238
Cdd:cd16874    10 FLDQIAKFWELQGCTLK-IPHVERKILDLFQLNKLVAEEGGFDLVCKERKWTKIATKMGFAPGKAVGSHIRAHYERILYP 88


                  .
gi 767943247  239 F 239
Cdd:cd16874    89 Y 89
ARID_ARID5B cd16885
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5B (ARID5B) ...
 155-248 1.72e-03

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.


Pssm-ID: 350649  Cd Length: 95  Bit Score: 38.90  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  155 ERKLWVDRYlTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNL--NVGTSSSAASSlKKQY 232
Cdd:cd16885     2 EQAFLVALY-KYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGYETITARRQWKHIYDELggNPGSTSAATCT-RRHY 79

                          90
                  ....*....|....*.
gi 767943247  233 IQYLFAFEcKIERGEE 248
Cdd:cd16885    80 ERLILPYE-RFIKGEE 94
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 423-576 2.54e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.10  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   423 DRRHEPYGQQYPGQGPPSGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGdmynmqyssQQQEMYNQYGGsysgpd 502
Cdd:TIGR01628  365 EQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPR---------MSMMPTPMGPG------ 429

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943247   503 rRPIQGQYPYPYSRERMQGPGQIQTHGIPPQMmggPLQSSSSEGPQQNMWAARNDMPYPYQNRQGPGGPTQ---APP 576
Cdd:TIGR01628  430 -GPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQ---PVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVlasATP 502
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 486-618 2.86e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.10  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247   486 QQQEMYNQYGG--SYSGPDRRPIQGQYPYPYSRERMQGPGQIQTHGIPPqMMGGPLQSSSSEGPqqnmwaarNDMPYPYQ 563
Cdd:TIGR01628  372 QDQFMQLQPRMrqLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMS-MMPTPMGPGGPLRP--------NGLAPMNA 442

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943247   564 NRQGPGGPTQAP------PYPGMNRTDDMMVPDQRINHESQwPSHVSQRQPYMSSSASMQP 618
Cdd:TIGR01628  443 VRAPSRNAQNAAqkppmqPVMYPPNYQSLPLSQDLPQPQST-ASQGGQNKKLAQVLASATP 502
PHA03377 PHA03377
EBNA-3C; Provisional
 256-680 8.28e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.81  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  256 TGDTKKQPKLQPPSPANSG---SLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQGGRSSTisvhDPFSDVSD 332
Cdd:PHA03377  543 SGRRQKRATPPKVSPSDRGppkASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPAS----GPHEKQPP 618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  333 SSFPKRNSMTPNAPYQQGMSMPDVMGRMP---YEPNKDPFG-GMRKVPGSSEPFMTQGQMPNSS---------MQDMYNQ 399
Cdd:PHA03377  619 SSAPRDMAPSVVRMFLRERLLEQSTGPKPksfWEMRAGRDGsGIQQEPSSRRQPATQSTPPRPSwlpsvfvlpSVDAGRA 698

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  400 SPSGAMSNLGMGQRQqfPYGASYDRRHEPYG-----QQYPGQGP-PSGQPPYGGHQPGLYPQQPnYKRHMDGMygPPAKR 473
Cdd:PHA03377  699 QPSEESHLSSMSPTQ--PISHEEQPRYEDPDdpldlSLHPDQAPpPSHQAPYSGHEEPQAQQAP-YPGYWEPR--PPQAP 773

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  474 HEGdmynMQYSSQQQEMYNQYGGsYSGPdrRPIQGQYP------YPYSRERMQGPGQiqthgippqmmgGPlqssssegp 547
Cdd:PHA03377  774 YLG----YQEPQAQGVQVSSYPG-YAGP--WGLRAQHPryrhswAYWSQYPGHGHPQ------------GP--------- 825

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943247  548 qqnmWAARNdmPYPyqnrqgpggPTQAPPYPGMNRTddmmvpdqrinhesqwpsHVSQRQPymsssasMQPITRPPQPSY 627
Cdd:PHA03377  826 ----WAPRP--PHL---------PPQWDGSAGHGQD------------------QVSQFPH-------LQSETGPPRLQL 865

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767943247  628 QTPPSLPNHI----SRAPSPASFQRSLENRMSPSKSPfLPSMKMQKVMPTVPTSQVT 680
Cdd:PHA03377  866 SQVPQLPYSQtlvsSSAPSWSSPQPRAPIRPIPTRFP-PPPMPLQDSMAVGCDSSGT 921
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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