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Conserved domains on  [gi|641679547|ref|XP_008188608|]
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trithorax group protein osa isoform X2 [Acyrthosiphon pisum]

Protein Classification

ARID/BRIGHT DNA-binding domain-containing protein( domain architecture ID 13013628)

ARID (AT-rich interactive domain)/BRIGHT DNA-binding domain-containing protein similar to Arabidopsis thaliana AT-rich interactive domain-containing protein 1 (ARID1) that is specifically required for sperm cell formation

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 ...
1717-1982 1.62e-144

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: 448.32  E-value: 1.62e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1717 SIGKRCVCISNILRNLSFVPGNELEFAKSGPFLGLVGKLLLTHHEHPLRSSKTRNYDKADDDTESLFNCTTttdadtiep 1796
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRD--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1797 gndaKWWWDYLDVVRENLLVSLANIAGYVDLSTFNEDISRPILDGLLHWAICPAAAGQDPFPS----APLSPQRLALESL 1872
Cdd:pfam12031   72 ----EWWWDCLEVLRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSagpnSPLSPQRLVLEAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1873 CKLCVTDNNVDLVIATPPYSRLEKLANVLTRLLCRTEEQVLREFAVNLLHYLAAADSGMARTIALQSPCVSLLVAFIEQT 1952
Cdd:pfam12031  148 CKLSVIDNNVDLILATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDA 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 641679547  1953 EQNALSVVNTHGLNALRDNPDSMGTSLDML 1982
Cdd:pfam12031  228 EQNAQYVQSQHGLNALRDNPELMGTSVDML 257
ARID_ARID1A-like cd16865
ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ...
957-1052 1.54e-53

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: 182.09  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 1036
Cdd:cd16865     1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAE---VTKNKKWKEICTELNIGASSSAAFTLRK 77
                          90
                  ....*....|....*.
gi 641679547 1037 HYTKNLLPYECHFDRG 1052
Cdd:cd16865    78 NYIKYLLAYECRFDRG 93
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1078-1453 7.40e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.57  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1078 PSPGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPqdynspqrPPHPPHGTQGSYQGQGGYSQQYPGGneqygqhyPPAS 1157
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPA--------PPAVPAGPATPGGPARPARPPTTAG--------PPAP 2769
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1158 TPVGYPSGPVRPPLYPP--YSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGR--GPVPPPSgyqqppRFPGPPPPQNS 1233
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPavASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPT------SAQPTAPPPPP 2843
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1234 SPATVNQTQGGSVStPGYPpgqqpqpdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPD-FAK--DQQAGPPQPAg 1310
Cdd:PHA03247 2844 GPPPPSLPLGGSVA-PGGD---------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALppDQPERPPQPQ- 2912
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1311 ypgygPQQRPMYPgpgwtgtpnaasnqyPRPGYPPGSQPPQnwsQGPPRSMPPSHPGQPPQweqhrypPQGQPYGAQQNH 1390
Cdd:PHA03247 2913 -----APPPPQPQ---------------PQPPPPPQPQPPP---PPPPRPQPPLAPTTDPA-------GAGEPSGAVPQP 2962
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641679547 1391 W-GPMAQAQMRMPRhgYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSI 1453
Cdd:PHA03247 2963 WlGALVPGRVAVPR--FRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSL 3024
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
485-643 8.83e-05

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.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 47.49  E-value: 8.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   485 SQQQPDQGQATQNNRMSHSPMGPQQGYQQQPSPQPPGGMPHMTGPSSGAPGNPYkmpgpnpygppppvsshsGYPAQQPA 564
Cdd:TIGR01628  361 AQRKEQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPL------------------GWPRMSMM 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   565 PPmGSYPQQPPGNygarppglpyQGYPPPNSNGPPQQYSPRGMPMHHGPPHQFPP-YQGWPGSGPPQAPPPlnNSHHSGP 643
Cdd:TIGR01628  423 PT-PMGPGGPLRP----------NGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPnYQSLPLSQDLPQPQS--TASQGGQ 489
 
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 ...
1717-1982 1.62e-144

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: 448.32  E-value: 1.62e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1717 SIGKRCVCISNILRNLSFVPGNELEFAKSGPFLGLVGKLLLTHHEHPLRSSKTRNYDKADDDTESLFNCTTttdadtiep 1796
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRD--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1797 gndaKWWWDYLDVVRENLLVSLANIAGYVDLSTFNEDISRPILDGLLHWAICPAAAGQDPFPS----APLSPQRLALESL 1872
Cdd:pfam12031   72 ----EWWWDCLEVLRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSagpnSPLSPQRLVLEAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1873 CKLCVTDNNVDLVIATPPYSRLEKLANVLTRLLCRTEEQVLREFAVNLLHYLAAADSGMARTIALQSPCVSLLVAFIEQT 1952
Cdd:pfam12031  148 CKLSVIDNNVDLILATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDA 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 641679547  1953 EQNALSVVNTHGLNALRDNPDSMGTSLDML 1982
Cdd:pfam12031  228 EQNAQYVQSQHGLNALRDNPELMGTSVDML 257
ARID_ARID1A-like cd16865
ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ...
957-1052 1.54e-53

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: 182.09  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 1036
Cdd:cd16865     1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAE---VTKNKKWKEICTELNIGASSSAAFTLRK 77
                          90
                  ....*....|....*.
gi 641679547 1037 HYTKNLLPYECHFDRG 1052
Cdd:cd16865    78 NYIKYLLAYECRFDRG 93
BRIGHT smart00501
BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a ...
957-1051 5.69e-32

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: 120.46  E-value: 5.69e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547    957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEVCkvtKNKIWKDVAGLLGIGA-SSSAAYTLR 1035
Cdd:smart00501    1 RERVLFLDRLYKFMEERGSPLKKIPVIGGKPLDLYRLYRLVQERGGYDQVT---KDKKWKEIARELGIPDtSTSAASSLR 77
                            90
                    ....*....|....*.
gi 641679547   1036 KHYTKNLLPYECHFDR 1051
Cdd:smart00501   78 KHYERYLLPYERFLRG 93
ARID pfam01388
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ...
958-1046 1.95e-28

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: 110.41  E-value: 1.95e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 1036
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYD---KVTEKNLWREVAEKLGFPPSaASAATQLKQ 77
                           90
                   ....*....|
gi 641679547  1037 HYTKNLLPYE 1046
Cdd:pfam01388   78 IYEKYLLPYE 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
1078-1453 7.40e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.57  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1078 PSPGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPqdynspqrPPHPPHGTQGSYQGQGGYSQQYPGGneqygqhyPPAS 1157
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPA--------PPAVPAGPATPGGPARPARPPTTAG--------PPAP 2769
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1158 TPVGYPSGPVRPPLYPP--YSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGR--GPVPPPSgyqqppRFPGPPPPQNS 1233
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPavASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPT------SAQPTAPPPPP 2843
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1234 SPATVNQTQGGSVStPGYPpgqqpqpdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPD-FAK--DQQAGPPQPAg 1310
Cdd:PHA03247 2844 GPPPPSLPLGGSVA-PGGD---------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALppDQPERPPQPQ- 2912
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1311 ypgygPQQRPMYPgpgwtgtpnaasnqyPRPGYPPGSQPPQnwsQGPPRSMPPSHPGQPPQweqhrypPQGQPYGAQQNH 1390
Cdd:PHA03247 2913 -----APPPPQPQ---------------PQPPPPPQPQPPP---PPPPRPQPPLAPTTDPA-------GAGEPSGAVPQP 2962
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641679547 1391 W-GPMAQAQMRMPRhgYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSI 1453
Cdd:PHA03247 2963 WlGALVPGRVAVPR--FRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSL 3024
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1080-1432 1.05e-08

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.55  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1080 PGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYSQQYPggnEQYGQHYPPASTP 1159
Cdd:pfam03154  172 PVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTP---TLHPQRLPSPHPP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1160 VGYPSGPVRPPLYPPYSNDADRNYGgsvPPPQGPPNTPQGPGNGQDPYgrgpvpPPSGYQQPPRFPGPPPPQNSSPATVN 1239
Cdd:pfam03154  249 LQPMTQPPPPSQVSPQPLPQPSLHG---QMPPMPHSLQTGPSHMQHPV------PPQPFPLTPQSSQSQVPPGPSPAAPG 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1240 QTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQR 1319
Cdd:pfam03154  320 QSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP-----PHLSGPSPFQMNSNLPPPP 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1320 PMYPgpgwtgtPNAASNQYPRPGYPPgsqPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPyGAQQNHWGPmaqAQM 1399
Cdd:pfam03154  395 ALKP-------LSSLSTHHPPSAHPP---PLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHP-PTSGLHQVP---SQS 460
                          330       340       350
                   ....*....|....*....|....*....|...
gi 641679547  1400 RMPRHGYRPDGSKPYGPhgPMAPPPHMKAGMPG 1432
Cdd:pfam03154  461 PFPQHPFVPGGPPPITP--PSGPPTSTSSAMPG 491
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
485-643 8.83e-05

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: 47.49  E-value: 8.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   485 SQQQPDQGQATQNNRMSHSPMGPQQGYQQQPSPQPPGGMPHMTGPSSGAPGNPYkmpgpnpygppppvsshsGYPAQQPA 564
Cdd:TIGR01628  361 AQRKEQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPL------------------GWPRMSMM 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   565 PPmGSYPQQPPGNygarppglpyQGYPPPNSNGPPQQYSPRGMPMHHGPPHQFPP-YQGWPGSGPPQAPPPlnNSHHSGP 643
Cdd:TIGR01628  423 PT-PMGPGGPLRP----------NGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPnYQSLPLSQDLPQPQS--TASQGGQ 489
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
477-634 2.89e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  477 PMPPRPPSSQQQPDQGQATQNNRMSHSPMGPQQGYQQQPSPQPPGGMPHMTGPSSGAPGNPYKMPGPNPYGPPPPVSShS 556
Cdd:PRK07764  610 EEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP-A 688
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641679547  557 GYPAQQPAPPMGSYPQQPPGNYGARPPGLPYQGYPPPNSNGPPQQYSPRGMPMHHGPPHQFPPYQGWPGSGPPQAPPP 634
Cdd:PRK07764  689 APAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1268-1400 1.50e-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: 43.64  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1268 ASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQRPMYPGpgwtgTPNAAsnQYPRPgYPPGS 1347
Cdd:TIGR01628  378 LQPRMRQLPMGSPMGGAMGQPPYYGQGP-----QQQFNGQPLGWPRMSMMPTPMGPG-----GPLRP--NGLAP-MNAVR 444
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 641679547  1348 QPPQNWSQGPPRSMPPSHPgQPPQWEQHRYPPQGQPYGAQQNHWGPMAQ-AQMR 1400
Cdd:TIGR01628  445 APSRNAQNAAQKPPMQPVM-YPPNYQSLPLSQDLPQPQSTASQGGQNKKlAQVL 497
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
559-647 2.84e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.72  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   559 PAQQPAPPMGSYPQQPPGnygarPPGLPYQGYPPPNSNGPPQQYSPRGMPMHHGPPHQFPPYQGwPGSGPPQAPPPlnns 638
Cdd:pfam09770  210 PAQQPAPAPAQPPAAPPA-----QQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQR-PQSPQPDPAQP---- 279

                   ....*....
gi 641679547   639 hHSGPVQPP 647
Cdd:pfam09770  280 -SIQPQAQQ 287
 
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 ...
1717-1982 1.62e-144

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: 448.32  E-value: 1.62e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1717 SIGKRCVCISNILRNLSFVPGNELEFAKSGPFLGLVGKLLLTHHEHPLRSSKTRNYDKADDDTESLFNCTTttdadtiep 1796
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRD--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1797 gndaKWWWDYLDVVRENLLVSLANIAGYVDLSTFNEDISRPILDGLLHWAICPAAAGQDPFPS----APLSPQRLALESL 1872
Cdd:pfam12031   72 ----EWWWDCLEVLRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSagpnSPLSPQRLVLEAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1873 CKLCVTDNNVDLVIATPPYSRLEKLANVLTRLLCRTEEQVLREFAVNLLHYLAAADSGMARTIALQSPCVSLLVAFIEQT 1952
Cdd:pfam12031  148 CKLSVIDNNVDLILATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDA 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 641679547  1953 EQNALSVVNTHGLNALRDNPDSMGTSLDML 1982
Cdd:pfam12031  228 EQNAQYVQSQHGLNALRDNPELMGTSVDML 257
ARID_ARID1A-like cd16865
ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ...
957-1052 1.54e-53

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: 182.09  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 1036
Cdd:cd16865     1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAE---VTKNKKWKEICTELNIGASSSAAFTLRK 77
                          90
                  ....*....|....*.
gi 641679547 1037 HYTKNLLPYECHFDRG 1052
Cdd:cd16865    78 NYIKYLLAYECRFDRG 93
ARID_ARID1B cd16877
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) ...
957-1052 3.15e-32

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: 121.25  E-value: 3.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGfmeVCKVTKNKIWKDVAGLLGIGASSSAAYTLRK 1036
Cdd:cd16877     1 PERKLWVDRYLTFMEERGTPVASLPAVGKKPLDLFRLYVCVKEIGG---LAQVNKNKKWRELATNLNVGTSSSAASSLKK 77
                          90
                  ....*....|....*.
gi 641679547 1037 HYTKNLLPYECHFDRG 1052
Cdd:cd16877    78 QYIQYLFAFECKIERG 93
BRIGHT smart00501
BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a ...
957-1051 5.69e-32

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: 120.46  E-value: 5.69e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547    957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEVCkvtKNKIWKDVAGLLGIGA-SSSAAYTLR 1035
Cdd:smart00501    1 RERVLFLDRLYKFMEERGSPLKKIPVIGGKPLDLYRLYRLVQERGGYDQVT---KDKKWKEIARELGIPDtSTSAASSLR 77
                            90
                    ....*....|....*.
gi 641679547   1036 KHYTKNLLPYECHFDR 1051
Cdd:smart00501   78 KHYERYLLPYERFLRG 93
ARID smart01014
ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction ...
957-1046 3.66e-29

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: 112.32  E-value: 3.66e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547    957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGI-GASSSAAYTLR 1035
Cdd:smart01014    1 RERELFLDRLRKFMEKRGTPLDKIPVIGGKPLDLYRLYRAVQKRGGFD---KVTKKKKWKQVARELGIpPSATSAGTSLR 77
                            90
                    ....*....|.
gi 641679547   1036 KHYTKNLLPYE 1046
Cdd:smart01014   78 KHYEKYLLPYE 88
ARID pfam01388
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ...
958-1046 1.95e-28

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: 110.41  E-value: 1.95e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 1036
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYD---KVTEKNLWREVAEKLGFPPSaASAATQLKQ 77
                           90
                   ....*....|
gi 641679547  1037 HYTKNLLPYE 1046
Cdd:pfam01388   78 IYEKYLLPYE 87
ARID_ARID3 cd16867
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID3A, ...
949-1047 2.02e-28

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: 111.42  E-value: 2.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  949 KLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGAS- 1027
Cdd:cd16867     3 QLYELSDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYRLVVEKGGLVE---VINKKIWREITKGLNLPSSi 79
                          90       100
                  ....*....|....*....|
gi 641679547 1028 SSAAYTLRKHYTKNLLPYEC 1047
Cdd:cd16867    80 TSAAFTLRTQYMKYLYPYEC 99
ARID_ARID1A cd16876
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1A (ARID1A) ...
957-1052 8.71e-27

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: 105.90  E-value: 8.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  957 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 1036
Cdd:cd16876     1 PERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQ---VNKNKKWRELATNLNVGTSSSAASSLKK 77
                          90
                  ....*....|....*.
gi 641679547 1037 HYTKNLLPYECHFDRG 1052
Cdd:cd16876    78 QYIQCLYAFECKIERG 93
ARID cd16100
ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of ...
958-1046 2.46e-25

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: 101.28  E-value: 2.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 1036
Cdd:cd16100     1 EREEFLEQLRAFLESRGTPLLKPPTIGGKPLDLYKLYRAVVSRGGYE---KVTEKKLWKEVARKLGLPTSsTSAAQALKR 77
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16100    78 IYEKYLLPFE 87
ARID_ARID3B cd16879
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3B (ARID3B) ...
947-1047 1.63e-24

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: 100.47  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  947 LSKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGA 1026
Cdd:cd16879     3 FAKLYELDNDPKRKEFLDDLFAFMQKRGTPINRIPIMAKQVLDLYMLYKLVTEKGGLVE---VINKKIWREITKGLNLPT 79
                          90       100
                  ....*....|....*....|..
gi 641679547 1027 S-SSAAYTLRKHYTKNLLPYEC 1047
Cdd:cd16879    80 SiTSAAFTLRTQYMKYLYPYEC 101
ARID_ARID3C cd16880
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3C (ARID3C) ...
945-1047 8.72e-24

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: 98.57  E-value: 8.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  945 DSLSKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGI 1024
Cdd:cd16880     2 EQFKQLYELDDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYTLYRLVTDKGGLVE---VINKKIWREITKGLSL 78
                          90       100
                  ....*....|....*....|....
gi 641679547 1025 GAS-SSAAYTLRKHYTKNLLPYEC 1047
Cdd:cd16880    79 PTSiTSAAFTLRTQYMKYLYPYEC 102
ARID_Dri-like cd16881
ARID/BRIGHT DNA binding domain of dead ringer (Dri) from Drosophila melanogaster and similar ...
948-1047 2.16e-23

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: 97.27  E-value: 2.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  948 SKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGAS 1027
Cdd:cd16881     9 KQLYEISDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYNLVVARGGLVE---VINKKLWREITKGLHLPSS 85
                          90       100
                  ....*....|....*....|.
gi 641679547 1028 -SSAAYTLRKHYTKNLLPYEC 1047
Cdd:cd16881    86 iTSAAFTLRTQYMKYLYPYEC 106
ARID_ARID3A cd16878
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3A (ARID3A) ...
945-1056 2.26e-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: 97.44  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  945 DSLSKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGI 1024
Cdd:cd16878     9 EQFKQLYELDGDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYMLYVLVTEKGGLVE---VINKKLWREITKGLNL 85
                          90       100       110
                  ....*....|....*....|....*....|...
gi 641679547 1025 GAS-SSAAYTLRKHYTKNLLPYECHfDRGGIDP 1056
Cdd:cd16878    86 PTSiTSAAFTLRTQYMKYLYPYECE-KRGLSNP 117
ARID_ARID5 cd16869
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID5A, ...
958-1046 5.08e-17

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: 77.72  E-value: 5.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASS-SAAYTLRK 1036
Cdd:cd16869     1 EEQAFLKLLYKFMKDRGTPIERIPHLGFKQIDLYTFFKLVQKLGGYEQ---VTAKRLWKHVYDELGGNPSStSAATCTRR 77
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16869    78 HYEKLLLPYE 87
ARID_HMGB9-like cd16872
ARID/BRIGHT DNA binding domain of Arabidopsis thaliana high mobility group B proteins HMGB9, ...
958-1046 3.02e-16

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: 75.38  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPiSTCPTISKNPLDLFRLYIYVKERGGfMEvcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 1036
Cdd:cd16872     1 DPDLFWETLRKFHESLGTK-FRIPIVGGKELDLHRLYKEVTSRGG-LE--KVIKDRKWKEVAAVFNFPPTiTNASFVLRK 76
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16872    77 YYLSLLHHYE 86
ARID_ARID4 cd16868
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID4A, ...
958-1046 1.30e-15

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: 73.58  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGA-SSSAAYTLRK 1036
Cdd:cd16868     1 EKENFLEQLYKFMEDRGTPINKPPVLGYKDLDLFKLYKLVQELGGME---RVSQGAKWRSIYQQLGIPVlNSAASHNIKQ 77
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16868    78 AYKKYLYAFE 87
ARID_JARID cd16864
ARID/BRIGHT DNA binding domain of JARID proteins; The JARID subfamily within the JmjC protein ...
963-1046 7.46e-13

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: 65.79  E-value: 7.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  963 LDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCKVTKnkiWKDVAGLLGIGASSSAAYTLRKHYTKNL 1042
Cdd:cd16864     8 LDQIAKFWELQGSSLKI-PNVERKALDLFTLHKIVQEEGGFEEVTKERK---WSKVARRLGYPPGKGVGSLLRGHYERIL 83

                  ....
gi 641679547 1043 LPYE 1046
Cdd:cd16864    84 YPYD 87
ARID_Swi1p-like cd16871
ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and ...
963-1046 6.88e-12

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: 63.42  E-value: 6.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  963 LDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGI--GASSSAAYTLRKHYTK 1040
Cdd:cd16871     7 MKSLREFMAKRGTPIEQQPVIGGRPVNLFRLYQLVQKLGGSR---QVTQNNQWPRVAQKLGFppEQNPQVAQQLAQIYQR 83

                  ....*.
gi 641679547 1041 NLLPYE 1046
Cdd:cd16871    84 YLLPYE 89
ARID_ARID5A cd16884
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5A (ARID5A) ...
958-1046 1.44e-11

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: 62.33  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIG-ASSSAAYTLRK 1036
Cdd:cd16884     1 EEQAFLVNLYKFMKERNTPIERIPHLGFKQINLWKIYKAVEKLGGYE---LVTARRLWKNVYDELGGSpGSTSAATCTRR 77
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16884    78 HYERLVLPYV 87
ARID_ARID2 cd16866
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and ...
958-1046 6.07e-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: 60.36  E-value: 6.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 1036
Cdd:cd16866     1 EYDAFLNELRQFHASRGTPFKKIPVVGGKELDLYLLYSKVTALGGWA---KVTDKNKWEEILEDFNFPRGcSNAAFALKQ 77
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16866    78 IYLRYLEAYE 87
ARID_ARID4B cd16883
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4B (ARID4B) ...
958-1046 8.81e-11

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: 60.37  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGASSSAA-YTLRK 1036
Cdd:cd16883     1 ERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFD---NIESGAVWKQVYQDLGIPVLNSAAgYNVKC 77
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16883    78 AYRKYLYGFE 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
1078-1453 7.40e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.57  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1078 PSPGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPqdynspqrPPHPPHGTQGSYQGQGGYSQQYPGGneqygqhyPPAS 1157
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPA--------PPAVPAGPATPGGPARPARPPTTAG--------PPAP 2769
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1158 TPVGYPSGPVRPPLYPP--YSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGR--GPVPPPSgyqqppRFPGPPPPQNS 1233
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPavASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPT------SAQPTAPPPPP 2843
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1234 SPATVNQTQGGSVStPGYPpgqqpqpdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPD-FAK--DQQAGPPQPAg 1310
Cdd:PHA03247 2844 GPPPPSLPLGGSVA-PGGD---------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALppDQPERPPQPQ- 2912
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1311 ypgygPQQRPMYPgpgwtgtpnaasnqyPRPGYPPGSQPPQnwsQGPPRSMPPSHPGQPPQweqhrypPQGQPYGAQQNH 1390
Cdd:PHA03247 2913 -----APPPPQPQ---------------PQPPPPPQPQPPP---PPPPRPQPPLAPTTDPA-------GAGEPSGAVPQP 2962
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641679547 1391 W-GPMAQAQMRMPRhgYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSI 1453
Cdd:PHA03247 2963 WlGALVPGRVAVPR--FRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSL 3024
ARID_KDM5C_5D cd16875
ARID/BRIGHT DNA binding domain of lysine-specific demethylase KDM5C and KDM5D; This group ...
962-1046 4.20e-09

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: 55.31  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  962 WLDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCkvtKNKIWKDVAGLLGIGASSSAAYTLRKHYTKN 1041
Cdd:cd16875     7 YLDQIAKFWEIQGSSLKI-PNVERRILDLYSLSKIVQEEGGYEAIC---KDRRWARVAQRLGYPPGKNIGSLLRSHYERI 82

                  ....*
gi 641679547 1042 LLPYE 1046
Cdd:cd16875    83 IYPYE 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
1078-1483 5.94e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.88  E-value: 5.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1078 PSPGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSP--QRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYGQHYPP 1155
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPppERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR 2686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1156 ASTP-VGYPSGPVRPPLYPPYSNDADRNYGGSVpppqGPPNTPQGPGNGQDPYGRGPVPPPSgyqqppRFPGPPPPQNSS 1234
Cdd:PHA03247 2687 AARPtVGSLTSLADPPPPPPTPEPAPHALVSAT----PLPPGPAAARQASPALPAAPAPPAV------PAGPATPGGPAR 2756
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1235 PATVNQTQGGSVSTPGYPPGQQPQP----------DYYRQEPPASPGYPPTSAPGTYPGKGMPP---PQPRRHPDFAKDQ 1301
Cdd:PHA03247 2757 PARPPTTAGPPAPAPPAAPAAGPPRrltrpavaslSESRESLPSPWDPADPPAAVLAPAAALPPaasPAGPLPPPTSAQP 2836
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1302 QAGPPQPAGYPGYGPQQRPMYPG-----PGWTGTPNAASNQYPRP-----GYPPGSQPPQNWSQGPPRSMPPSHPGQPPq 1371
Cdd:PHA03247 2837 TAPPPPPGPPPPSLPLGGSVAPGgdvrrRPPSRSPAAKPAAPARPpvrrlARPAVSRSTESFALPPDQPERPPQPQAPP- 2915
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1372 weqhryPPQGQPYGAQQNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQpmfqgSSLMKREVIFPPD 1451
Cdd:PHA03247 2916 ------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR-----VAVPRFRVPQPAP 2984
                         410       420       430
                  ....*....|....*....|....*....|..
gi 641679547 1452 SIEAVTPILYKRRrmmRHDVAPVDAWRLMMSL 1483
Cdd:PHA03247 2985 SREAPASSTPPLT---GHSLSRVSSWASSLAL 3013
ARID_KDM5A cd16873
ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5A (KDM5A); KDM5A, also called ...
962-1046 7.11e-09

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: 54.89  E-value: 7.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  962 WLDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCKvtkNKIWKDVAGLLGIGASSSAAYTLRKHYTKN 1041
Cdd:cd16873     7 FLDQLAKFWELQGSTLKI-PVVERKILDLYALSKIVASEGGFEMVTK---EKKWSKVGSRMGYLPGKGTGSLLKSHYERI 82

                  ....*
gi 641679547 1042 LLPYE 1046
Cdd:cd16873    83 LYPYE 87
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1080-1432 1.05e-08

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.55  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1080 PGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYSQQYPggnEQYGQHYPPASTP 1159
Cdd:pfam03154  172 PVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTP---TLHPQRLPSPHPP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1160 VGYPSGPVRPPLYPPYSNDADRNYGgsvPPPQGPPNTPQGPGNGQDPYgrgpvpPPSGYQQPPRFPGPPPPQNSSPATVN 1239
Cdd:pfam03154  249 LQPMTQPPPPSQVSPQPLPQPSLHG---QMPPMPHSLQTGPSHMQHPV------PPQPFPLTPQSSQSQVPPGPSPAAPG 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1240 QTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQR 1319
Cdd:pfam03154  320 QSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP-----PHLSGPSPFQMNSNLPPPP 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1320 PMYPgpgwtgtPNAASNQYPRPGYPPgsqPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPyGAQQNHWGPmaqAQM 1399
Cdd:pfam03154  395 ALKP-------LSSLSTHHPPSAHPP---PLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHP-PTSGLHQVP---SQS 460
                          330       340       350
                   ....*....|....*....|....*....|...
gi 641679547  1400 RMPRHGYRPDGSKPYGPhgPMAPPPHMKAGMPG 1432
Cdd:pfam03154  461 PFPQHPFVPGGPPPITP--PSGPPTSTSSAMPG 491
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1236-1424 2.92e-08

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 59.07  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1236 ATVNQTQGGSVSTPGYPPgQQPQPDYYRQEPPASPGYPPTSA----PGTYPGKGMPPPQPRrHPDFAKDQQAGPPQPAGY 1311
Cdd:PRK14086   86 ITVDPSAGEPAPPPPHAR-RTSEPELPRPGRRPYEGYGGPRAddrpPGLPRQDQLPTARPA-YPAYQQRPEPGAWPRAAD 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1312 PgYGPQQRPMYPGPgwtGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPG----QPPQWEQHRypPQGQPYGAQ 1387
Cdd:PRK14086  164 D-YGWQQQRLGFPP---RAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRpdwdRPRRDRTDR--PEPPPGAGH 237
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 641679547 1388 QNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPP 1424
Cdd:PRK14086  238 VHRGGPGPPERDDAPVVPIRPSAPGPLAAQPAPAPGP 274
ARID_KDM5B cd16874
ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5B (KDM5B); KDM5B, also called ...
962-1045 8.50e-08

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: 51.86  E-value: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  962 WLDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCKVTKnkiWKDVAGLLGIGASSSAAYTLRKHYTKN 1041
Cdd:cd16874    10 FLDQIAKFWELQGCTLKI-PHVERKILDLFQLNKLVAEEGGFDLVCKERK---WTKIATKMGFAPGKAVGSHIRAHYERI 85

                  ....
gi 641679547 1042 LLPY 1045
Cdd:cd16874    86 LYPY 89
ARID_ARID4A cd16882
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4A (ARID4A) ...
958-1046 1.42e-07

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: 51.13  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGfmevC-KVTKNKIWKDVAGLLGIGA-SSSAAYTLR 1035
Cdd:cd16882     1 ERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYQQGG----CdNIESGSVWKQIYMDLGIPIlNSAASYNVK 76
                          90
                  ....*....|.
gi 641679547 1036 KHYTKNLLPYE 1046
Cdd:cd16882    77 TAYRKYLYGFE 87
ARID_ARID5B cd16885
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5B (ARID5B) ...
958-1046 3.23e-07

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: 50.07  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  958 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFmEVckVTKNKIWKDVAGLLGIG-ASSSAAYTLRK 1036
Cdd:cd16885     1 DEQAFLVALYKYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGY-ET--ITARRQWKHIYDELGGNpGSTSAATCTRR 77
                          90
                  ....*....|
gi 641679547 1037 HYTKNLLPYE 1046
Cdd:cd16885    78 HYERLILPYE 87
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1208-1388 1.24e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.84  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1208 GRGPVPPPSGYQQPPRFPGPPPPQNSSPATVNQTQGGSVSTPGYPPGQQPQPdyyrqepPASPGYPPTSAPGTYPGKGmP 1287
Cdd:PRK07764  595 AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPG-------VAAPEHHPKHVAVPDASDG-G 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1288 PPQPRRHPDFAKDQQAGPPQPAGYPG-YGPQQRPMYPGPGWT---GTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPP 1363
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAApAGAAPAQPAPAPAATppaGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
                         170       180
                  ....*....|....*....|....*
gi 641679547 1364 SHPGQPPQWEQHRYPPQGQPYGAQQ 1388
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPAAAPA 771
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1154-1376 1.57e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.45  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1154 PPASTPVGYPSGPVRPPLYPPYSNDADrnyggsvpppqgpPNTPQGPGNGQDPYGRGPVPPPSGYQQPPRFPGPPPPQNS 1233
Cdd:PRK07764  600 PPAPASSGPPEEAARPAAPAAPAAPAA-------------PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1234 SPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRrhpdfakdQQAGPPQPAGYPG 1313
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA--------QGASAPSPAADDP 738
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641679547 1314 YGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPqnWSQGPPRSMPPSHPGQPPQWEQHR 1376
Cdd:PRK07764  739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP--PSPPSEEEEMAEDDAPSMDDEDRR 799
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
1080-1434 1.71e-06

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: 53.41  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1080 PGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYsqqYPGGNEQYGQ----HYPP 1155
Cdd:pfam03157  224 PERGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGY---YPTSLQQPGQgqsgYYPT 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1156 ASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQG--PGNGQDP-YGRGPVPPPSGYQQPPRFPGPPPPQN 1232
Cdd:pfam03157  301 SQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQQPAQGqqPGQGQPGyYPTSPQQPGQGQPGYYPTSQQQPQQG 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1233 SSPATVNQTQGGSVSTPGYPPGQQPQPDYYRQ-EPPASPGYPPTSAPGTYP------GKGMPPPQPRR--HPDFAKDQQA 1303
Cdd:pfam03157  381 QQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPgYYPTSPQQSGQGQPGYYPtspqqsGQGQQPGQGQQpgQEQPGQGQQP 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1304 GPPQPAGYPGYGPQ-QRPMYPGPGWTGTPNAASNQYPRPGY-------PPGSQP--PQNWSQGPPRSMP--PSHPGQPPQ 1371
Cdd:pfam03157  461 GQGQQGQQPGQPEQgQQPGQGQPGYYPTSPQQSGQGQQLGQwqqqgqgQPGYYPtsPLQPGQGQPGYYPtsPQQPGQGQQ 540
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641679547  1372 WEQHRYPPQGQP-----YGAQQNHWGPMAQAQMR-------MPRHGYRPDGSKP-YGPHGPMAPPPHMKAGMPGQP 1434
Cdd:pfam03157  541 LGQLQQPTQGQQgqqsgQGQQGQQPGQGQQGQQPgqgqqgqQPGQGQQPGQGQPgYYPTSPQQSGQGQQPGQWQQP 616
PHA03378 PHA03378
EBNA-3B; Provisional
1235-1434 4.46e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.99  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1235 PATVNQTQGGSVSTPGYP--PGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMP-PPQPRRHPDFAKDQQAGPPqpagy 1311
Cdd:PHA03378  576 PLTSPTTSQLASSAPSYAqtPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPiPMRPLRMQPITFNVLVFPT----- 650
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1312 PGYGPQQRPMYPGPGWTGTPNAASNqyPRPGYPPGSQPPQnWS----QGPPRS---MPPSH----PGQPPQWEQHRYPPq 1380
Cdd:PHA03378  651 PHQPPQVEITPYKPTWTQIGHIPYQ--PSPTGANTMLPIQ-WApgtmQPPPRAptpMRPPAappgRAQRPAAATGRARP- 726
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 641679547 1381 gqPYGAQQNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPphmkAGMPGQP 1434
Cdd:PHA03378  727 --PAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPP----AAAPGAP 774
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1205-1383 4.92e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 4.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1205 DPYGRGPVPPPSGYQQPPRFPGPPPPQNSSPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTyPGK 1284
Cdd:PRK07764  616 AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPA-APA 694
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1285 GMPPPQPrrhpdfakdQQAGPPQPAGYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPgsqPPQNWSQGPPRSMPPS 1364
Cdd:PRK07764  695 GAAPAQP---------APAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD---DPPDPAGAPAQPPPPP 762
                         170
                  ....*....|....*....
gi 641679547 1365 HPGQPPQWEQHRYPPQGQP 1383
Cdd:PRK07764  763 APAPAAAPAAAPPPSPPSE 781
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1243-1451 5.27e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.53  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1243 GGSVSTPGYPPGQQPQPdyyrQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMY 1322
Cdd:PRK07764  599 GPPAPASSGPPEEAARP----AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAG 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1323 PGPGWTGTPNAASNQYPRPGYPPGSQPpqnwsqGPPRSMPPSHPGQPPQWEQHRYPPQGQpygaqqnhWGPMAQAQMRMP 1402
Cdd:PRK07764  675 GAAPAAPPPAPAPAAPAAPAGAAPAQP------APAPAATPPAGQADDPAAQPPQAAQGA--------SAPSPAADDPVP 740
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 641679547 1403 RHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPD 1451
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
1075-1382 6.98e-06

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: 51.49  E-value: 6.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1075 TSVPSPGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSP---QRPPHPPHGTQGSYQGQG--GY---SQQYPGGN 1146
Cdd:pfam03157  417 TSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPgqgQQGQQPGQPEQGQQPGQGqpGYyptSPQQSGQG 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1147 EQYGQHYPPASTPVG-YPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGRGPVPPPSGYQQPPRFP 1225
Cdd:pfam03157  497 QQLGQWQQQGQGQPGyYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQ 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1226 GPPPPQNSSPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSApgTYPGKGMPPPQPrrhpdfAKDQQAGP 1305
Cdd:pfam03157  577 GQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSS--LQLGQGQQGYYP------TSPQQPGQ 648
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1306 -PQPAGYPGYGPQQRPMYPgpgwTGTPNAASNQYPRPGYPPGS--QPPQNWSQGPPRSmpPSHPGQPPQWEQHRYPPQGQ 1382
Cdd:pfam03157  649 gQQPGQWQQSGQGQQGYYP----TSPQQSGQAQQPGQGQQPGQwlQPGQGQQGYYPTS--PQQPGQGQQLGQGQQSGQGQ 722
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1232-1439 8.50e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.03  E-value: 8.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1232 NSSPATVNQTQGGSVSTPGYPP-GQQPQPDYYRQEPPASPGY-PPTSAPGTYPGKGMPPP---QPRRHPDFAKDQQAGPP 1306
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAPaAAAPAPAAPPAAPAAAPAAaAAARAVAAAPARRSPAPealAAARQASARGPGGAPAP 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1307 QPAGYPGYGPQQRPMYPGPgwtGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPqweqhrYPPQGQPYGA 1386
Cdd:PRK12323  451 APAPAAAPAAAARPAAAGP---RPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAP------AQPDAAPAGW 521
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 641679547 1387 QQNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQ------PMFQGS 1439
Cdd:PRK12323  522 VAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAsasglpDMFDGD 580
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1258-1463 1.15e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 50.80  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1258 QPDYYRQEPPASPGYPPTSapgtypgkgmPPPQPRRHPDFAKDQQAGPPQPA--GY-----PGYGPQQRPMYPGPGWTGT 1330
Cdd:pfam09770   99 QVRFNRQQPAARAAQSSAQ----------PPASSLPQYQYASQQSQQPSKPVrtGYekykePEPIPDLQVDASLWGVAPK 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1331 PNAASNQYPRPGYPPGSQPPQN---------------WSQGPPRSMPPSHPGQPPQWEQHRYPPQGQ--PYGAQQNHWGP 1393
Cdd:pfam09770  169 KAAAPAPAPQPAAQPASLPAPSrkmmsleeveaamraQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQfpPQIQQQQQPQQ 248
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641679547  1394 MAQAQMRMPRHGY------RPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSIEAVTPILYKR 1463
Cdd:pfam09770  249 QPQQPQQHPGQGHpvtilqRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGV 324
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1242-1370 1.33e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1242 QGGSVSTPGYPPGQQPQPDyyRQEPPAspgypPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGP-PQPAGYPGYGPQQRP 1320
Cdd:PRK07764  383 RRLGVAGGAGAPAAAAPSA--AAAAPA-----AAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPaPPSPAGNAPAGGAPS 455
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 641679547 1321 MYPGPGWTGTPNAASNQYPRPGYPPGSQPPqNWSQGPPRSMPPSHPGQPP 1370
Cdd:PRK07764  456 PPPAAAPSAQPAPAPAAAPEPTAAPAPAPP-AAPAPAAAPAAPAAPAAPA 504
PHA03378 PHA03378
EBNA-3B; Provisional
1154-1424 1.61e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1154 PPASTPvgypsGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQdpygrGPVPPPSGYQQPPRFPGPPPPQNS 1233
Cdd:PHA03378  696 PPPRAP-----TPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAP-----GRARPPAAAPGRARPPAAAPGRAR 765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1234 SPATvnqTQGGSVSTP----GYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPpqPA 1309
Cdd:PHA03378  766 PPAA---APGAPTPQPppqaPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRP--SL 840
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1310 GYPGYGPQQRPMYPGPGWTGTPNAASNQYPrPGYPPGSQPPQ-NWSQGPPRSMPPSHPGQPPqweqhryppqgQPYGAQQ 1388
Cdd:PHA03378  841 KKPAALERQAAAGPTPSPGSGTSDKIVQAP-VFYPPVLQPIQvMRQLGSVRAAAASTVTQAP-----------TEYTGER 908
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 641679547 1389 NHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPP 1424
Cdd:PHA03378  909 RGVGPMHPTDIPPSKRAKTDAYVESQPPHGGQSHSF 944
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1248-1447 2.52e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1248 TPGYPPGQQPQPdyyRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMYPGPGW 1327
Cdd:PRK07764  616 AAPAAPAAPAAP---APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1328 TGTPNAASNQYPRPGYPPGSQPPQNWSQgPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQmrMPRHGYR 1407
Cdd:PRK07764  693 PAGAAPAQPAPAPAATPPAGQADDPAAQ-PPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPP--APAPAAA 769
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 641679547 1408 PDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVI 1447
Cdd:PRK07764  770 PAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMELL 809
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1266-1434 3.34e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1266 PPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYP--GYGPQQRPMYPGPGWTGTPNAASNQYPRPGy 1343
Cdd:PRK07764  593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEAsaAPAPGVAAPEHHPKHVAVPDASDGGDGWPA- 671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1344 PPGSQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQMRMPRHGYRPDG-SKPYGPHGPMAP 1422
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPvPLPPEPDDPPDP 751
                         170
                  ....*....|..
gi 641679547 1423 PPHMKAGMPGQP 1434
Cdd:PRK07764  752 AGAPAQPPPPPA 763
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1244-1398 4.84e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.49  E-value: 4.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1244 GSVSTPGYPPGQQPQPdyyrqePPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAkdQQAGPPQPAgypgYGPQQRPMYP 1323
Cdd:pfam09770  209 KPAQQPAPAPAQPPAA------PPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHP--GQGHPVTIL----QRPQSPQPDP 276
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641679547  1324 GPGWTGTPNAASNQYPRPGYPPGSQPPQNwsqgpPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQ 1398
Cdd:pfam09770  277 AQPSIQPQAQQFHQQPPPVPVQPTQILQN-----PNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPII 346
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1234-1434 4.88e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.49  E-value: 4.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1234 SPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPP-----TSAPGTYPGKgmpPPQPRRHPDFAKdQQAGPPQP 1308
Cdd:pfam09770  114 SSAQPPASSLPQYQYASQQSQQPSKPVRTGYEKYKEPEPIPdlqvdASLWGVAPKK---AAAPAPAPQPAA-QPASLPAP 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1309 ---------------AGYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWE 1373
Cdd:pfam09770  190 srkmmsleeveaamrAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRP 269
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641679547  1374 QHRYPPQGQPYGAQQNHWGPMAQAQMRM---------PRHGYRPDGSKPYGPHGPMAPPPHM----KAGMPGQP 1434
Cdd:pfam09770  270 QSPQPDPAQPSIQPQAQQFHQQPPPVPVqptqilqnpNRLSAARVGYPQNPQPGVQPAPAHQahrqQGSFGRQA 343
PHA03247 PHA03247
large tegument protein UL36; Provisional
1200-1458 5.02e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1200 PGNGQDPYGRGP----VPPPSGYQQPPRFPGPPPPQNSSPATVNQTQG---------GSVSTPGYPPGQQPQPDyyRQEP 1266
Cdd:PHA03247 2492 AGAAPDPGGGGPpdpdAPPAPSRLAPAILPDEPVGEPVHPRMLTWIRGleelasddaGDPPPPLPPAAPPAAPD--RSVP 2569
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1267 PASPG-YPPTSAPGTYPGKGMPPPQPR--RHPDFAKDQQAGPPQPAGYPGYGPQQRPmyPGPGwtgtPNAASNQYPRPGY 1343
Cdd:PHA03247 2570 PPRPApRPSEPAVTSRARRPDAPPQSArpRAPVDDRGDPRGPAPPSPLPPDTHAPDP--PPPS----PSPAANEPDPHPP 2643
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1344 PPGSQPPQNWSQ-GPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAqaqmrmprhgyrpDGSKPYGPHGPMAP 1422
Cdd:PHA03247 2644 PTVPPPERPRDDpAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLT-------------SLADPPPPPPTPEP 2710
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 641679547 1423 PPHmkAGMPGQPMFQGSSLMKREviFPPDSIEAVTP 1458
Cdd:PHA03247 2711 APH--ALVSATPLPPGPAAARQA--SPALPAAPAPP 2742
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
485-643 8.83e-05

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: 47.49  E-value: 8.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   485 SQQQPDQGQATQNNRMSHSPMGPQQGYQQQPSPQPPGGMPHMTGPSSGAPGNPYkmpgpnpygppppvsshsGYPAQQPA 564
Cdd:TIGR01628  361 AQRKEQRRAHLQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPL------------------GWPRMSMM 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   565 PPmGSYPQQPPGNygarppglpyQGYPPPNSNGPPQQYSPRGMPMHHGPPHQFPP-YQGWPGSGPPQAPPPlnNSHHSGP 643
Cdd:TIGR01628  423 PT-PMGPGGPLRP----------NGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPnYQSLPLSQDLPQPQS--TASQGGQ 489
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1241-1383 1.35e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.39  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1241 TQGGSVSTPGYPPGQ-----QPQPDYYRQEP---PASPGYPPTSAPGTYPGKGMPP---PQPRRHPDFAKDQQAGPPQPA 1309
Cdd:PRK10263  341 TQTPPVASVDVPPAQptvawQPVPGPQTGEPviaPAPEGYPQQSQYAQPAVQYNEPlqqPVQPQQPYYAPAAEQPAQQPY 420
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641679547 1310 GYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQP 1383
Cdd:PRK10263  421 YAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEP 494
PHA03247 PHA03247
large tegument protein UL36; Provisional
1078-1434 1.56e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1078 PSPGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSP--QRPPHPPhgtqgsyqgqggysqqypggneqygqhyPP 1155
Cdd:PHA03247 2578 SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPpdTHAPDPP----------------------------PP 2629
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1156 ASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPygRGPVPP--PSGYQQPPRFPGPPPPQNS 1233
Cdd:PHA03247 2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP--QRPRRRaaRPTVGSLTSLADPPPPPPT 2707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1234 SPATVNQTQGGSVSTPGYPPGQQPQPdyyrqEPPASPGYPPTSAPGTYPGKGMPPPQPR-----RHPDFAKDQQAGPPQP 1308
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASP-----ALPAAPAPPAVPAGPATPGGPARPARPPttagpPAPAPPAAPAAGPPRR 2782
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1309 AGYPGYGP--QQRPMYPGPGWTGTPNAA---------SNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHP---GQPPQWEQ 1374
Cdd:PHA03247 2783 LTRPAVASlsESRESLPSPWDPADPPAAvlapaaalpPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggSVAPGGDV 2862
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641679547 1375 HRYPPQGQPYGAQQNHWGPMAQaqmRMPRHGY-RPDGSKPYGPHGPmAPPPHMKAGMPGQP 1434
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPPVR---RLARPAVsRSTESFALPPDQP-ERPPQPQAPPPPQP 2919
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1265-1383 1.64e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.00  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1265 EPPASPGYPPTSAPgTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGypgygPQQRPMYPGPgwtgtPNAASNQYPRPGYP 1344
Cdd:PRK10263  742 EPLFTPIVEPVQQP-QQPVAPQQQYQQPQQPVAPQPQYQQPQQPVA-----PQPQYQQPQQ-----PVAPQPQYQQPQQP 810
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 641679547 1345 pgsQPPQNWSQGPPRSMPPshpgqPPQWEQHRYPPQGQP 1383
Cdd:PRK10263  811 ---VAPQPQYQQPQQPVAP-----QPQYQQPQQPVAPQP 841
ARID_JARD2 cd16870
ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and ...
970-1045 1.64e-04

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: 42.98  E-value: 1.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641679547  970 MEERGSPISTCPTISKNPLDLFRLYIYVKERGGfMEvcKVTKNKIWKDVAGLLGIGASSSAAYT-LRKHYTKNLLPY 1045
Cdd:cd16870    16 LESQGINLTPPPLIGGCELDLPRLYHLVQELGG-MQ--QVTDKKKWNKVADHLNIPKTAQDRPSkLQDAYCKYLLSY 89
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
477-634 2.89e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  477 PMPPRPPSSQQQPDQGQATQNNRMSHSPMGPQQGYQQQPSPQPPGGMPHMTGPSSGAPGNPYKMPGPNPYGPPPPVSShS 556
Cdd:PRK07764  610 EEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP-A 688
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641679547  557 GYPAQQPAPPMGSYPQQPPGNYGARPPGLPYQGYPPPNSNGPPQQYSPRGMPMHHGPPHQFPPYQGWPGSGPPQAPPP 634
Cdd:PRK07764  689 APAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766
PHA03264 PHA03264
envelope glycoprotein D; Provisional
1248-1369 1.00e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 43.84  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1248 TPGYP-PGQQPQPDYY-----RQEPP---ASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQq 1318
Cdd:PHA03264  231 TQYYPqEAHKAIVDYWfmrhgGVVPPyfeESKGYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPE- 309
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 641679547 1319 rpmypgpgwTGTPNAASNQYPRPGyPPGSQP----PQNWSQGPPRSMPPSHPGQP 1369
Cdd:PHA03264  310 ---------PAGRDGAAGGEPKPG-PPRPAPdadrPEGWPSLEAITFPPPTPATP 354
dnaA PRK14086
chromosomal replication initiator protein DnaA;
529-644 1.14e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 44.05  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  529 PSSGAPGNPYKMPGPNPYGPPPPVSSHSGYPAQQPAPPMGSYPqQPPGNYGarpPGLPYQGYPPPNSNGPPQQYSPR--- 605
Cdd:PRK14086  117 PYEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRPEPGAWP-RAADDYG---WQQQRLGFPPRAPYASPASYAPEqer 192
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 641679547  606 -GMPMHHGPPHQFPPYQGWPGSGP------------PQAPPPLNNSHHSGPV 644
Cdd:PRK14086  193 dREPYDAGRPEYDQRRRDYDHPRPdwdrprrdrtdrPEPPPGAGHVHRGGPG 244
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1080-1369 1.41e-03

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: 43.84  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1080 PGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYGQHYPPASTP 1159
Cdd:pfam09606  151 PGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMN 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1160 VGYPSG--PVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQD-PYGRGPVPPPSGYQQPPRFPGPPPPQNSSPA 1236
Cdd:pfam09606  231 PQQMGGapNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGgPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQ 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1237 TVNQTQGGSVSTPGYPPGQQPQP--DYYRQEPPASPGYPPTSAPGTYPGKGMPPPQP-----RRHPDFAKDQQAGPPQPA 1309
Cdd:pfam09606  311 TRQQQQQQGGNHPAAHQQQMNQSvgQGGQVVALGGLNHLETWNPGNFGGLGANPMQRgqpgmMSSPSPVPGQQVRQVTPN 390
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641679547  1310 GYPGYGPQQRPMYP-GPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQP 1369
Cdd:pfam09606  391 QFMRQSPQPSVPSPqGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGS 451
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1268-1400 1.50e-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: 43.64  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1268 ASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQRPMYPGpgwtgTPNAAsnQYPRPgYPPGS 1347
Cdd:TIGR01628  378 LQPRMRQLPMGSPMGGAMGQPPYYGQGP-----QQQFNGQPLGWPRMSMMPTPMGPG-----GPLRP--NGLAP-MNAVR 444
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 641679547  1348 QPPQNWSQGPPRSMPPSHPgQPPQWEQHRYPPQGQPYGAQQNHWGPMAQ-AQMR 1400
Cdd:TIGR01628  445 APSRNAQNAAQKPPMQPVM-YPPNYQSLPLSQDLPQPQSTASQGGQNKKlAQVL 497
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
1256-1400 1.85e-03

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 42.26  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1256 QPQPDYYRQEPPASPGYPPTSAPGtypgkgMPPPQPRRHPDFAKDQQ---AGPPQP--AGYPGYGPQQR--PMYPGPGWT 1328
Cdd:pfam07271  126 EPTEQQNTAEPTQPAGVNVANQPQ------MGINQPQINPQFGPNPQqriGFPMQPnmGMRPGFNQMPGmpPNQMRPGFN 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547  1329 GTPNAAsnqyPRPGYP---PGSQP-----PQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQMR 1400
Cdd:pfam07271  200 QMPGMP----PRPGFPnpmPNMQPrpgfrPQPGPMGNRPGGGFPHPGTPMGPNRMPNPGMNQRPGMAPPRPGFPPQNGPR 275
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1304-1499 2.51e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1304 GPPQPAGYPGYGPQQRPMypgpgwtgTPNAASNQYPRPGYPPgsqPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQP 1383
Cdd:PRK10263  739 GPHEPLFTPIVEPVQQPQ--------QPVAPQQQYQQPQQPV---APQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 807
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1384 ygaQQnhwgPMA-QAQMRMPRHGYRPdgSKPYG-PHGPMAPPPHMKAGMPgQPMFQGSSLMKREVIFPPDSIEAVTPily 1461
Cdd:PRK10263  808 ---QQ----PVApQPQYQQPQQPVAP--QPQYQqPQQPVAPQPQDTLLHP-LLMRNGDSRPLHKPTTPLPSLDLLTP--- 874
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 641679547 1462 krrrmMRHDVAPVDAWRL--MMSLRSGLLAESTWALDVLN 1499
Cdd:PRK10263  875 -----PPSEVEPVDTFALeqMARLVEARLADFRIKADVVN 909
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1268-1424 2.73e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1268 ASPGYPPTSAPgTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYP-GYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPG 1346
Cdd:PRK10263  334 AAPVEPVTQTP-PVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPeGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAA 412
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641679547 1347 SQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPyGAQQNHWGPMAQAQmrmPRHGYRPDGSKPYGPHGPMAPPP 1424
Cdd:PRK10263  413 EQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQA-EEQQSTFAPQSTYQ---TEQTYQQPAAQEPLYQQPQPVEQ 486
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
559-647 2.84e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.72  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547   559 PAQQPAPPMGSYPQQPPGnygarPPGLPYQGYPPPNSNGPPQQYSPRGMPMHHGPPHQFPPYQGwPGSGPPQAPPPlnns 638
Cdd:pfam09770  210 PAQQPAPAPAQPPAAPPA-----QQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQR-PQSPQPDPAQP---- 279

                   ....*....
gi 641679547   639 hHSGPVQPP 647
Cdd:pfam09770  280 -SIQPQAQQ 287
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1074-1350 3.01e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1074 ATSVPSPGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDynsPQRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYGQHY 1153
Cdd:PHA03307  165 DAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPR---PPRRSSPISASASSPAPAPGRSAADDAGASSSDSSS 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1154 PPASTPVGYPSGpvRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPyGRGPVPPPSGYQQPPRFPGPPPPQN- 1232
Cdd:PHA03307  242 SESSGCGWGPEN--ECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPR-ERSPSPSPSSPGSGPAPSSPRASSSs 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1233 --------SSPATVNQTQGGSVSTPGYPPGQQPQPDyyRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAG 1304
Cdd:PHA03307  319 sssresssSSTSSSSESSRGAAVSPGPSPSRSPSPS--RPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAG 396
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 641679547 1305 PPQPAGYPGYGPQQRPMYPGPGWTGTPNAASNQYPrPGYP-----PGSQPP 1350
Cdd:PHA03307  397 RARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP-LLTPsgepwPGSPPP 446
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1134-1379 3.21e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1134 GQGGYSQQYPGGNEQYGQHYPPASTPVGYPSGPVRPPLYPPysndadrnyggsVPPPQGPPNTPQGPGNGQDPYGRGPVP 1213
Cdd:PRK12323  367 QSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPA------------AAPAAAAAARAVAAAPARRSPAPEALA 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1214 PPSGYQQPprfpgppppqnsspatvnqtQGGSVSTPGYPPGQQPQPdyyRQEPPASPGYPPTSAPGTYPGKGMPPPQPRR 1293
Cdd:PRK12323  435 AARQASAR--------------------GPGGAPAPAPAPAAAPAA---AARPAAAGPRPVAAAAAAAPARAAPAAAPAP 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1294 HPDFAKDQQAGPPQPAGYPGYgpQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWE 1373
Cdd:PRK12323  492 ADDDPPPWEELPPEFASPAPA--QPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS 569

                  ....*.
gi 641679547 1374 QHRYPP 1379
Cdd:PRK12323  570 ASGLPD 575
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1248-1349 3.49e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1248 TPGYPPGQQPQpdyyrQEPPASPGYPPTSAPGTYPGKGMPPPQPrrhpdFAKDQQAGPPQP--AGYPGYGPQQRPMYPGP 1325
Cdd:PRK10263  746 TPIVEPVQQPQ-----QPVAPQQQYQQPQQPVAPQPQYQQPQQP-----VAPQPQYQQPQQpvAPQPQYQQPQQPVAPQP 815
                          90       100
                  ....*....|....*....|....*.
gi 641679547 1326 GWTG--TPNAASNQYPRPGYPPGSQP 1349
Cdd:PRK10263  816 QYQQpqQPVAPQPQYQQPQQPVAPQP 841
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
1273-1350 3.66e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 42.12  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1273 PPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQpagYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPG--------YP 1344
Cdd:PRK13729  127 PVTATGEPVPQMPASPPGPEGEPQPGNTPVSFPPQ---GSVAVPPPTAFYPGNGVTPPPQVTYQSVPVPNriqrktftYN 203

                  ....*.
gi 641679547 1345 PGSQPP 1350
Cdd:PRK13729  204 EGKKGP 209
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1303-1440 5.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1303 AGPPQPAGYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWS-QGPPRSMPPSHPGQPPQWEQHRYPPQG 1381
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASaAPAPGVAAPEHHPKHVAVPDASDGGDG 668
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 641679547 1382 QPYGAQQNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSS 1440
Cdd:PRK07764  669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG 727
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1154-1371 6.70e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1154 PPASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGRGPVPPP--SGYQQPPRFPGPPPPQ 1231
Cdd:PHA03307   71 PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPdlSEMLRPVGSPGPPPAA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641679547 1232 NSSPATVNQTQGGSvSTPGYPPGQQPQPdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGY 1311
Cdd:PHA03307  151 SPPAAGASPAAVAS-DAASSRQAALPLS--SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRS 227
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641679547 1312 PGYGPQQRPM-YPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQ 1371
Cdd:PHA03307  228 AADDAGASSSdSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS 288
 
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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