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Conserved domains on  [gi|212276472|sp|P51531|]
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RecName: Full=Probable global transcription activator SNF2L2; AltName: Full=ATP-dependent helicase SMARCA2; AltName: Full=BRG1-associated factor 190B; Short=BAF190B; AltName: Full=Protein brahma homolog; Short=hBRM; AltName: Full=SNF2-alpha; AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 701-951 6.98e-175

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


:

Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 524.24  E-value: 6.98e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  701 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 780
Cdd:cd18063     1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  781 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 860
Cdd:cd18063    81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  861 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 940
Cdd:cd18063   161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240

                         250
                  ....*....|.
gi 212276472  941 VLRPFLLRRLK 951
Cdd:cd18063   241 VLRPFLLRRLK 251
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
 720-1202 3.38e-164

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 524.75  E-value: 3.38e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  800 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 875
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 955
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  956 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1034
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1035 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1114
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1115 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1194
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615


                  ....*...
gi 212276472 1195 DQKVIQAG 1202
Cdd:PLN03142  616 DALVIQQG 623
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1382-1506 1.01e-58

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


:

Pssm-ID: 99947  Cd Length: 107  Bit Score: 197.26  E-value: 1.01e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKD------------------SDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 212276472 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05516    63 RSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQKI 107
HSA smart00573
domain in helicases and associated with SANT domains;
436-508 3.67e-24

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 97.47  E-value: 3.67e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276472    436 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 508
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
 1259-1326 4.29e-22

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


:

Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 91.17  E-value: 4.29e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472  1259 DRRREDARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1326
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
 589-632 3.26e-16

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


:

Pssm-ID: 462196  Cd Length: 44  Bit Score: 73.70  E-value: 3.26e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 212276472   589 QMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 632
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 173-207 1.52e-12

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


:

Pssm-ID: 462622  Cd Length: 35  Bit Score: 63.12  E-value: 1.52e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 212276472   173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Bromodomain super family cl02556
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 1333-1419 2.96e-11

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


The actual alignment was detected with superfamily member cd05494:

Pssm-ID: 445827 [Multi-domain]  Cd Length: 114  Bit Score: 62.08  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1333 NLEEMEEEVRLKKRKRRrNVDKDPAKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDT-VINYKDRCNVEKVPSNSQ 1411
Cdd:cd05494     1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETgARDLEDLQIVQEDPADKQ 77


                  ....*...
gi 212276472 1412 LEIEGNSS 1419
Cdd:cd05494    78 IDDEGRRS 85
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 46-450 1.05e-06

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.62  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    46 PSPGPPSVSHPMPTmgstdfPQEGMHQMHKPidGIHdkgivedihcgSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPHP 125
Cdd:pfam03154  253 TQPPPPSQVSPQPL------PQPSLHGQMPP--MPH-----------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   126 SPLGApeHVSSPMSGGGPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSPV------QLHQLRAQILA---YKMLARGQ 196
Cdd:pfam03154  314 SPAAP--GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIpqlpnpQSHKHPPHLSGpspFQMNSNLP 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   197 PLPETLQLAvqgkrtlpglqqqqqqqqqqqqqqqqqqqqqqqpqqqppqpqtqqqqqpALVNYNRPSGPGPELSGPSTPQ 276
Cdd:pfam03154  392 PPPALKPLS-------------------------------------------------SLSTHHPPSAHPPPLQLMPQSQ 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   277 KLPVP---APGGRPSPAPPAAAQPPAAAVPGPSVP-QP-------APGQPSPVLQLQQKQSRISP----IQKPQG----- 336
Cdd:pfam03154  423 QLPPPpaqPPVLTQSQSLPPPAASHPPTSGLHQVPsQSpfpqhpfVPGGPPPITPPSGPPTSTSSampgIQPPSSasvss 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   337 -----------LDPVEILQEreyrlqariahRIQELENlPGSLPPDLR------TKATVELKALRLLNFQRQLRQEVVAC 399
Cdd:pfam03154  503 sgpvpaavscpLPPVQIKEE-----------ALDEAEE-PESPPPPPRspspepTVVNTPSHASQSARFYKHLDRGYNSC 570

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472   400 MRRDTTLETALNSK-------AYKRSKRQTLREARMTEKLEKQQKIEQERKR-RQKHQE 450
Cdd:pfam03154  571 ARTDLYFMPLAGSKlakkreeALEKAKREAEQKAREEKEREKEKEKEREREReREREAE 629
 
Name Accession Description Interval E-value
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 701-951 6.98e-175

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 524.24  E-value: 6.98e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  701 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 780
Cdd:cd18063     1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  781 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 860
Cdd:cd18063    81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  861 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 940
Cdd:cd18063   161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240

                         250
                  ....*....|.
gi 212276472  941 VLRPFLLRRLK 951
Cdd:cd18063   241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 720-1202 3.38e-164

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 524.75  E-value: 3.38e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  800 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 875
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 955
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  956 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1034
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1035 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1114
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1115 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1194
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615


                  ....*...
gi 212276472 1195 DQKVIQAG 1202
Cdd:PLN03142  616 DALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 720-1186 3.06e-122

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 399.21  E-value: 3.06e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:COG0553   238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  800 VKISYKGTPAmRRSLVPQLRsgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRR 876
Cdd:COG0553   317 RVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHR 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtgervdlNEEETILIIRRLHKVLRPFLLRRLKKEVES 956
Cdd:COG0553   390 LALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----------IEKGDEEALERLRRLLRPFLLRRTKEDVLK 459

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  957 QLPEKVEYVIKCDMSALQKILYRHMQAKgillTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHlgys 1036
Cdd:COG0553   460 DLPEKTEETLYVELTPEQRALYEAVLEY----LRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR---- 531

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1037 ngvingaelyraSGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEpG 1116
Cdd:COG0553   532 ------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-G 598

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1117 SQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1186
Cdd:COG0553   599 PEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 727-1022 3.44e-113

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 359.30  E-value: 3.44e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   727 YQLQGLEWMVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRLNGPYLIIVPLSTLSNWTYEFDKWA--PSVVKI 802
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   803 SYKGTP-AMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTG 881
Cdd:pfam00176   81 VLHGNKrPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   882 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetiLIIRRLHKVLRPFLLRRLKKEVESQLPEK 961
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212276472   962 VEYVIKCDMSALQKILY-RHMQAKGILLTDGSEkdkKGKGGAKTLMNTIMQLRKICNHPYMF 1022
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1382-1506 1.01e-58

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 197.26  E-value: 1.01e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKD------------------SDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 212276472 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05516    63 RSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 1049-1175 1.54e-56

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.92  E-value: 1.54e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1049 SGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPgSQYFIFLLSTRA 1128
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 212276472 1129 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1175
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
723-912 4.38e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 4.38e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    723 TLKHYQLQGLEWMvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKrlNGPYLIIVPLSTL-SNWTYEFDKWAPS-V 799
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    800 VKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPR 875
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162

                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 212276472    876 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 912
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
BROMO smart00297
bromo domain;
1381-1506 2.11e-28

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 110.45  E-value: 2.11e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   1381 PKLTKQMNAIIDTVINYKDRcnvekvpsnsqleiegnssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHK 1460
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--------------------HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGK 61

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 212276472   1461 YRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:smart00297   62 YSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 1050-1164 6.10e-28

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 109.22  E-value: 6.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  1050 GKFELLDRILPKLRatNHRVLLFCQMTSlmTIMEDYFAFR-NFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRA 1128
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 212276472  1129 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIG 1164
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HSA smart00573
domain in helicases and associated with SANT domains;
436-508 3.67e-24

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 97.47  E-value: 3.67e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276472    436 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 508
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
 1259-1326 4.29e-22

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 91.17  E-value: 4.29e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472  1259 DRRREDARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1326
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HELICc smart00490
helicase superfamily c-terminal domain;
1081-1164 6.50e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.12  E-value: 6.50e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   1081 IMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRA 1160
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                    ....
gi 212276472   1161 HRIG 1164
Cdd:smart00490   79 GRAG 82
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
 437-503 5.90e-21

HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 88.01  E-value: 5.90e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212276472   437 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERM 503
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1412-1492 5.49e-20

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 85.83  E-value: 5.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:pfam00439    2 LEILDKLMEHPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKA 81


                   .
gi 212276472  1492 S 1492
Cdd:pfam00439   82 A 82
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
 589-632 3.26e-16

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 462196  Cd Length: 44  Bit Score: 73.70  E-value: 3.26e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 212276472   589 QMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 632
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
590-632 1.86e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 1.86e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 212276472    590 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 632
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPR 43
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1412-1501 4.49e-14

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 76.00  E-value: 4.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:COG5076   154 KKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVD 233

                          90
                  ....*....|
gi 212276472 1492 SIVLQSVFKS 1501
Cdd:COG5076   234 AKELEKYFLK 243
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 173-207 1.52e-12

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 462622  Cd Length: 35  Bit Score: 63.12  E-value: 1.52e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 212276472   173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
 1333-1419 2.96e-11

Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99926 [Multi-domain]  Cd Length: 114  Bit Score: 62.08  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1333 NLEEMEEEVRLKKRKRRrNVDKDPAKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDT-VINYKDRCNVEKVPSNSQ 1411
Cdd:cd05494     1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETgARDLEDLQIVQEDPADKQ 77


                  ....*...
gi 212276472 1412 LEIEGNSS 1419
Cdd:cd05494    78 IDDEGRRS 85
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
 172-206 6.26e-10

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 55.62  E-value: 6.26e-10
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 212276472    172 SPFSPVQLHQLRAQILAYK-MLARGQPLPETLQLAV 206
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 46-450 1.05e-06

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: 53.62  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    46 PSPGPPSVSHPMPTmgstdfPQEGMHQMHKPidGIHdkgivedihcgSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPHP 125
Cdd:pfam03154  253 TQPPPPSQVSPQPL------PQPSLHGQMPP--MPH-----------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   126 SPLGApeHVSSPMSGGGPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSPV------QLHQLRAQILA---YKMLARGQ 196
Cdd:pfam03154  314 SPAAP--GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIpqlpnpQSHKHPPHLSGpspFQMNSNLP 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   197 PLPETLQLAvqgkrtlpglqqqqqqqqqqqqqqqqqqqqqqqpqqqppqpqtqqqqqpALVNYNRPSGPGPELSGPSTPQ 276
Cdd:pfam03154  392 PPPALKPLS-------------------------------------------------SLSTHHPPSAHPPPLQLMPQSQ 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   277 KLPVP---APGGRPSPAPPAAAQPPAAAVPGPSVP-QP-------APGQPSPVLQLQQKQSRISP----IQKPQG----- 336
Cdd:pfam03154  423 QLPPPpaqPPVLTQSQSLPPPAASHPPTSGLHQVPsQSpfpqhpfVPGGPPPITPPSGPPTSTSSampgIQPPSSasvss 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   337 -----------LDPVEILQEreyrlqariahRIQELENlPGSLPPDLR------TKATVELKALRLLNFQRQLRQEVVAC 399
Cdd:pfam03154  503 sgpvpaavscpLPPVQIKEE-----------ALDEAEE-PESPPPPPRspspepTVVNTPSHASQSARFYKHLDRGYNSC 570

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472   400 MRRDTTLETALNSK-------AYKRSKRQTLREARMTEKLEKQQKIEQERKR-RQKHQE 450
Cdd:pfam03154  571 ARTDLYFMPLAGSKlakkreeALEKAKREAEQKAREEKEREKEKEKEREREReREREAE 629
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
721-883 1.73e-05

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 49.25  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  721 NGTLKHYQLQGLE-WMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLngpyLIIVPLSTLSN-WTYEFDKWAPS 798
Cdd:COG1061    78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  799 VVKISYKgtpamrrslvpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVA 873
Cdd:COG1061   154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPA 213

                         170
                  ....*....|
gi 212276472  874 PRRILLTGTP 883
Cdd:COG1061   214 AYRLGLTATP 223
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 340-551 4.75e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  340 VEILQEREYRLQARIA-------HRIQELEnlpgslppDLRTKATVELKALRLLNFQRQLRQEVVAcmRRDTTLETALNS 412
Cdd:COG1196   283 LEEAQAEEYELLAELArleqdiaRLEERRR--------ELEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEE 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  413 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQK 492
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472  493 KETERIEKERMRRLMAEDEEGYRKLIDQKKDRRLAyLLQQTDEYVANLTNLVWEHKQAQ 551
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAA 490
PHA03378 PHA03378
EBNA-3B; Provisional
 66-382 5.96e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   66 PQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPMSGGGPTP 145
Cdd:PHA03378  529 PPQPRAGRRAPCVYTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWP 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  146 PQMPPSQPG-----ALIPgdpqAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGLQQQ 218
Cdd:PHA03378  599 VPHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPY 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  219 QQQQQQQQQQQQQQQQQQQQPQQQP--------PQPQTQQQQQPALVNYNRPSGPGPELSGPSTPQKLPVPAPGGRPSPA 290
Cdd:PHA03378  675 QPSPTGANTMLPIQWAPGTMQPPPRaptpmrppAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 754

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  291 PPAAAQPPAAAVPGPSVPQPAPGQP--SPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELENLPG 366
Cdd:PHA03378  755 RPPAAAPGRARPPAAAPGAPTPQPPpqAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGGVK 834

                         330
                  ....*....|....*.
gi 212276472  367 SLPPDLRTKATVELKA 382
Cdd:PHA03378  835 RGRPSLKKPAALERQA 850
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-525 1.25e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   333 KPQGLDPVEILQEREY-------RLQARIAHRIQELENLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTT 405
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   406 LETALnskAYKRSKRQTLRE--ARMTEKLEKQQKIEQERKRRQKHQEyLNSILQHAKDFKEYHRSVAGKIQKLskavatw 483
Cdd:TIGR02169  749 LEQEI---ENVKSELKELEAriEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSKLEEEVSRIEARLREI------- 817

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 212276472   484 hanterEQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRR 525
Cdd:TIGR02169  818 ------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
PTZ00121 PTZ00121
MAEBL; Provisional
 413-524 2.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  413 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHAntEREQK 492
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614

                          90       100       110
                  ....*....|....*....|....*....|..
gi 212276472  493 KETERIEKERMRRlmaedEEGYRKLIDQKKDR 524
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 43-170 2.67e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 41.95  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   43 MMGPSPGPPSVS-HPMPTMGSTDFPQEGMHQMHKPIDGIHdkgivEDIHCGSMKGTGMRPPHPGMGPPQSPmdQHSQGYM 121
Cdd:cd22056   195 MMAAGGGGFMGQqKPKHQMHSVHPQAFTHHQAAGPGALQG-----RGGRGGPDCHLLHSSHHHHHHHHLQY--QYMNAPY 267

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212276472  122 SPHPSPLGAP----------EHVS---SPMSGGGPTPPQMPPSQPgaLIPGDPQAMSQPNRG 170
Cdd:cd22056   268 PPHYAHQGAPqfhgqysvfrEPMRvhhQGHPGSMLTPPSSPPLLE--FYAQDEPEDIKPKRG 327
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 98-199 2.82e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.16  E-value: 2.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472     98 GMRPPH--PGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPMsgggptPPQMPPSQPGALIPGDPQAMSQPNrgpspfS 175
Cdd:smart00818   51 TLQPHHhiPVLPAQQPVVPQQPLMPVPGQHSMTPTQHHQPNLP------QPAQQPFQPQPLQPPQPQQPMQPQ------P 118

                            90       100
                    ....*....|....*....|....
gi 212276472    176 PVQLHQLRAQILAYKMLARGQPLP 199
Cdd:smart00818  119 PVHPIPPLPPQPPLPPMFPMQPLP 142
 
Name Accession Description Interval E-value
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 701-951 6.98e-175

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 524.24  E-value: 6.98e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  701 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 780
Cdd:cd18063     1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  781 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 860
Cdd:cd18063    81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  861 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 940
Cdd:cd18063   161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240

                         250
                  ....*....|.
gi 212276472  941 VLRPFLLRRLK 951
Cdd:cd18063   241 VLRPFLLRRLK 251
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 721-951 1.25e-169

DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 509.22  E-value: 1.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  721 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVV 800
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  801 KISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLT 880
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276472  881 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERV--DLNEEETILIIRRLHKVLRPFLLRRLK 951
Cdd:cd17996   161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 720-1202 3.38e-164

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 524.75  E-value: 3.38e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  800 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 875
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 955
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  956 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1034
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1035 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1114
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1115 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1194
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615


                  ....*...
gi 212276472 1195 DQKVIQAG 1202
Cdd:PLN03142  616 DALVIQQG 623
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 701-951 2.07e-162

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 491.10  E-value: 2.07e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  701 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 780
Cdd:cd18062     1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  781 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 860
Cdd:cd18062    81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  861 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 940
Cdd:cd18062   161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240

                         250
                  ....*....|.
gi 212276472  941 VLRPFLLRRLK 951
Cdd:cd18062   241 VLRPFLLRRLK 251
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 720-1186 3.06e-122

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 399.21  E-value: 3.06e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:COG0553   238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  800 VKISYKGTPAmRRSLVPQLRsgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRR 876
Cdd:COG0553   317 RVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHR 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtgervdlNEEETILIIRRLHKVLRPFLLRRLKKEVES 956
Cdd:COG0553   390 LALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----------IEKGDEEALERLRRLLRPFLLRRTKEDVLK 459

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  957 QLPEKVEYVIKCDMSALQKILYRHMQAKgillTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHlgys 1036
Cdd:COG0553   460 DLPEKTEETLYVELTPEQRALYEAVLEY----LRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR---- 531

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1037 ngvingaelyraSGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEpG 1116
Cdd:COG0553   532 ------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-G 598

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1117 SQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1186
Cdd:COG0553   599 PEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 727-1022 3.44e-113

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 359.30  E-value: 3.44e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   727 YQLQGLEWMVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRLNGPYLIIVPLSTLSNWTYEFDKWA--PSVVKI 802
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   803 SYKGTP-AMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTG 881
Cdd:pfam00176   81 VLHGNKrPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   882 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetiLIIRRLHKVLRPFLLRRLKKEVESQLPEK 961
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212276472   962 VEYVIKCDMSALQKILY-RHMQAKGILLTDGSEkdkKGKGGAKTLMNTIMQLRKICNHPYMF 1022
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 721-951 6.36e-92

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 297.38  E-value: 6.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  721 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrLNGPYLIIVPLSTLSNWTYEFDKWAPSVV 800
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  801 KISYKGTPAMRRSLVPQLRS-----GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPR 875
Cdd:cd18009    80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212276472  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN--APFAMTGERVDLNEEETILIIRRLHKVLRPFLLRRLK 951
Cdd:cd18009   159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 721-951 4.53e-90

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 291.53  E-value: 4.53e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  721 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVV 800
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  801 KISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvaprR 876
Cdd:cd17997    81 VVVLIGDKEERADIIrDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVrlfNSRN----R 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276472  877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamTGERVDLNEEetilIIRRLHKVLRPFLLRRLK 951
Cdd:cd17997   157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN-----VNNCDDDNQE----VVQRLHKVLRPFLLRRIK 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 724-949 1.70e-81

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 267.30  E-value: 1.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRslvpQLRSG-----KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRIL 878
Cdd:cd18003    81 YYGSAKERK----LKRQGwmkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212276472  879 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF-AMTGERVDLNEEetilIIRRLHKVLRPFLLRR 949
Cdd:cd18003   156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLtAMSEGSQEENEE----LVRRLHKVLRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 723-949 4.13e-79

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 260.37  E-value: 4.13e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  723 TLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKI 802
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  803 SYKGTPAMRRSL------VPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRR 876
Cdd:cd17993    81 VYLGDIKSRDTIreyefyFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276472  877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgerVDLNEEETILiIRRLHKVLRPFLLRR 949
Cdd:cd17993   160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 724-900 3.17e-78

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 255.95  E-value: 3.17e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYvAPRRILLTGTP 883
Cdd:cd17919    81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159

                         170
                  ....*....|....*..
gi 212276472  884 LQNKLPELWALLNFLLP 900
Cdd:cd17919   160 LQNNLEELWALLDFLDP 176
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 724-949 6.96e-73

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 242.54  E-value: 6.96e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVkIS 803
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMNV-VV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRR-----------SLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 871
Cdd:cd17995    80 YHGSGESRQiiqqyemyfkdAQGRKKKGvYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212276472  872 VAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 949
Cdd:cd17995   159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 711-961 3.65e-70

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 235.72  E-value: 3.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  711 RVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 790
Cdd:cd18064     3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  791 EFDKWAPSVVKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 869
Cdd:cd18064    83 EFKRWVPTLRAVCLIGDKDQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  870 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 949
Cdd:cd18064   162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRR 231

                         250
                  ....*....|..
gi 212276472  950 LKKEVESQLPEK 961
Cdd:cd18064   232 IKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 711-951 8.31e-70

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 234.14  E-value: 8.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  711 RVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 790
Cdd:cd18065     3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  791 EFDKWAPSVVKISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 869
Cdd:cd18065    83 EFKRWVPSLRAVCLIGDKDARAAFIrDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  870 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 949
Cdd:cd18065   162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 231


                  ..
gi 212276472  950 LK 951
Cdd:cd18065   232 IK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 724-949 2.50e-62

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 212.75  E-value: 2.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLVP-------QLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRR 876
Cdd:cd18002    81 YWGNPKDRKVLRKfwdrknlYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212276472  877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERV-DLNEEEtiliIRRLHKVLRPFLLRR 949
Cdd:cd18002   160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKtGLNEHQ----LKRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 724-949 2.74e-62

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 212.94  E-value: 2.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRI 877
Cdd:cd18054   101 YIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212276472  878 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGERVDLNEEEtiliirrLHKVLRPFLLRR 949
Cdd:cd18054   180 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLEPFLLRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 720-951 5.44e-62

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 211.27  E-value: 5.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  800 VKISYKGTPAMRRSLVpqlRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHYvaprR 876
Cdd:cd18012    80 KVLVIHGTKRKREKLR---ALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLKADH----R 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276472  877 ILLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGERvDLNEEEtiliIRRLHKVLRPFLLRRLK 951
Cdd:cd18012   153 LALTGTPIENHLGELWSIFDFLNPGLLGS----YKRFKKRFAKPIEK-DGDEEA----LEELKKLISPFILRRLK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 724-949 4.90e-60

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 205.36  E-value: 4.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVaPRRILLTGT 882
Cdd:cd18006    81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212276472  883 PLQNKLPELWALLNFLLPTIFkSCSTFEQWFNApFAMTGERVDLNEEetiliirrLHKVLRPFLLRR 949
Cdd:cd18006   160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1382-1506 1.01e-58

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 197.26  E-value: 1.01e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKD------------------SDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 212276472 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05516    63 RSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 1049-1175 1.54e-56

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.92  E-value: 1.54e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1049 SGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPgSQYFIFLLSTRA 1128
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 212276472 1129 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1175
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 724-949 1.08e-55

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 192.27  E-value: 1.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTpamrrslvpqlrsgkfNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRILLTGTP 883
Cdd:cd17994    81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212276472  884 LQNKLPELWALLNFLLPTIFKSCSTFeqwfnapfamTGERVDLNEEETiliIRRLHKVLRPFLLRR 949
Cdd:cd17994   144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 724-903 2.66e-53

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 184.90  E-value: 2.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRlNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLVPQLRSG--KFNVLLTTYEYII---KDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRIL 878
Cdd:cd17998    80 YYGSQEERKHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INANFRLL 158

                         170       180
                  ....*....|....*....|....*
gi 212276472  879 LTGTPLQNKLPELWALLNFLLPTIF 903
Cdd:cd17998   159 LTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 727-900 1.76e-50

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 177.13  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  727 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAP--------- 797
Cdd:cd18000     4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvvlhs 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  798 ---SVVKISYKGTPAMRRSLVPQLRsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNThy 871
Cdd:cd18000    84 sgsGTGSEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLRT-- 160

                         170       180
                  ....*....|....*....|....*....
gi 212276472  872 vaPRRILLTGTPLQNKLPELWALLNFLLP 900
Cdd:cd18000   161 --PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 724-949 9.05e-50

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 176.78  E-value: 9.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRI 877
Cdd:cd18053   101 YLGDINSRNMIRthewmhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212276472  878 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGERVDLNEEEtiliirrLHKVLRPFLLRR 949
Cdd:cd18053   180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 724-949 4.96e-49

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 174.46  E-value: 4.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKR------LNGPYLIIVPLSTLSNWTYEFDKWAP 797
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  798 SVVK--ISYKGTPAMRRSLVPQLrsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPR 875
Cdd:cd17999    80 NAFLkpLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212276472  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT--GERVDLNEEETILIIRRLHKVLRPFLLRR 949
Cdd:cd17999   157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASrdSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 724-949 2.97e-48

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 172.56  E-value: 2.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT-----------------YLMEHKRLN---GPYLIIVPLS 783
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrennrpRFKKKPPASsakKPVLIVAPLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  784 TLSNWTYEFDKWAPSVVKISYKGTPAMrrSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 863
Cdd:cd18005    81 VLYNWKDELDTWGHFEVGVYHGSRKDD--ELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  864 TQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF----AMTGERVDLNEEETilIIRRLH 939
Cdd:cd18005   159 TQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK--RKQELA 235

                         250
                  ....*....|
gi 212276472  940 KVLRPFLLRR 949
Cdd:cd18005   236 VKLSKFFLRR 245
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 724-949 6.14e-48

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 170.99  E-value: 6.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVkIS 803
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWTEMNA-IV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTpAMRRSLVPQLR-----------SG--KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTH 870
Cdd:cd18058    79 YHGS-QISRQMIQQYEmyyrdeqgnplSGifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLM 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472  871 YVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 949
Cdd:cd18058   158 ALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 724-949 2.21e-47

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 169.86  E-value: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLVPQ--------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 863
Cdd:cd18057    81 YTGDKESRSVIRENefsfednaIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  864 TQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgerVDLNEEETiliIRRLHKVLR 943
Cdd:cd18057   161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226


                  ....*.
gi 212276472  944 PFLLRR 949
Cdd:cd18057   227 PHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 724-949 1.77e-46

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 166.77  E-value: 1.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRLNGPYLIIVPLSTLSNWTYEFDKWApSVVKIS 803
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQE-VYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRR--------------SLVPQlrSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 869
Cdd:cd18060    79 YHGSLASRQmiqqyemyckdsrgRLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  870 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 949
Cdd:cd18060   156 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 724-949 1.83e-46

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 167.11  E-value: 1.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAmRRSLVPQ---------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCK 862
Cdd:cd18055    81 YTGDKD-SRAIIREnefsfddnaVKGGkkafkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  863 LTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgerVDLNEEETiliIRRLHKVL 942
Cdd:cd18055   160 FFRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLL 225


                  ....*..
gi 212276472  943 RPFLLRR 949
Cdd:cd18055   226 GPHMLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 727-949 1.88e-46

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 167.16  E-value: 1.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  727 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPyLIIVPLSTLSNWTYEFDKWAPSV-VKISYK 805
Cdd:cd18001     4 HQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLrVKVFHG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  806 GTPAMRRSlvpQLRS--GKFNVLLTTYEYIIKDKHILA-----KIRWKYMIVDEGHRMKNHHCKLTQVLntHYV-APRRI 877
Cdd:cd18001    83 TSKKERER---NLERiqRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAKNRI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  878 LLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPF-------AMTGERVDLNEeetilIIRRLHKVLRPFLLRR 949
Cdd:cd18001   158 ILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPItrgrdkdATQGEKALGSE-----VAENLRQIIKPYFLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 724-949 2.20e-45

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 163.66  E-value: 2.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVkIS 803
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV-VV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMRRSLV--------PQLR----SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHY 871
Cdd:cd18059    79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212276472  872 VApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 949
Cdd:cd18059   159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 724-949 3.18e-44

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 160.62  E-value: 3.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 YKGTPAMR--------------------RSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 863
Cdd:cd18056    81 YVGDKDSRaiirenefsfednairggkkASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  864 TQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgerVDLNEEETiliIRRLHKVLR 943
Cdd:cd18056   161 FRVLNG-YSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDMLG 226


                  ....*.
gi 212276472  944 PFLLRR 949
Cdd:cd18056   227 PHMLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 724-949 4.56e-43

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 157.45  E-value: 4.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVS--LYNNNLNG---ILADEMGLGKTIQTIALITYLMEHKRLNGP----YLIIVPLSTLSNWTYEFDK 794
Cdd:cd18004     1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  795 W----APSVVKISYKGTPAMRRSLvpQLRSGK-FNVLLTTYE-YIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 868
Cdd:cd18004    81 WlglrRIKVVTADGNAKDVKASLD--FFSSAStYPVLIISYEtLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  869 ThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvDLNEEETILIIRRLH---KVLRPF 945
Cdd:cd18004   159 S-LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRF 236


                  ....
gi 212276472  946 LLRR 949
Cdd:cd18004   237 ILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 724-949 1.50e-42

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 156.29  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLynnnlNGILADEMGLGKTIQTIALI------------TYLMEHKRLNGPY-----LIIVPLSTLS 786
Cdd:cd18008     1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeELEENSSDPKKLYlskttLIVVPLSLLS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  787 NWTYEFDK----WAPSVVKisYKGtpAMRRSLVPQLRSgkFNVLLTTY-----EY-----------IIKDKHILAKIRWK 846
Cdd:cd18008    76 QWKDEIEKhtkpGSLKVYV--YHG--SKRIKSIEELSD--YDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  847 YMIVDEGHRMKNHHCKLTQV---LNTHyvapRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFamtger 923
Cdd:cd18008   150 RVILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF------ 219

                         250       260
                  ....*....|....*....|....*.
gi 212276472  924 vdlnEEETILIIRRLHKVLRPFLLRR 949
Cdd:cd18008   220 ----SKNDRKALERLQALLKPILLRR 241
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 724-949 3.53e-41

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 151.70  E-value: 3.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTialITYLMEHKR--LNGPYLIIVPLSTLSNWTYEFDKWAPSVVk 801
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS---ITFLYEILLtgIRGPFLIIAPLSTIANWEREFRTWTDLNV- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  802 ISYKGTpAMRRSLVPQLR-------------SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 868
Cdd:cd18061    77 VVYHGS-LISRQMIQQYEmyfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  869 THYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLR 948
Cdd:cd18061   156 LMNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLR 221


                  .
gi 212276472  949 R 949
Cdd:cd18061   222 R 222
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 724-916 1.11e-36

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 139.35  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWM----VSLYNNNLNG---ILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWA 796
Cdd:cd18007     1 LKPHQVEGVRFLwsnlVGTDVGSDEGggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  797 PSVVkISYKGTPAMRRSLVPQLRSGKFN-------VLLTTYEY---IIKDKHILAKIRWKYM-----------IVDEGHR 855
Cdd:cd18007    81 PPDL-RPLLVLVSLSASKRADARLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEGHR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212276472  856 MKNHHCKLTQVLNTHYvAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAP 916
Cdd:cd18007   160 LKNEKSQLSKALSKVK-TKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKP 219
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 727-949 1.37e-32

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 127.59  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  727 YQLQGLEWMVSLYNNNL-----------------------------NGILADEMGLGKTIQTIALItylmehkrLNGPYL 777
Cdd:cd18071     4 HQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LANFTL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  778 IIVPLSTLSNWTYEF-DKWAPSVVKI-SYKGTpamRRSLVPQLRSGKfNVLLTTY-----EYIIKDKHILAKIRWKYMIV 850
Cdd:cd18071    76 IVCPLSVLSNWETQFeEHVKPGQLKVyTYHGG---ERNRDPKLLSKY-DIVLTTYntlasDFGAKGDSPLHTINWLRVVL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  851 DEGHRMKNHHCKLTQ-VLNTHyvAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLnee 929
Cdd:cd18071   152 DEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTGL--- 225

                         250       260
                  ....*....|....*....|
gi 212276472  930 etiliiRRLHKVLRPFLLRR 949
Cdd:cd18071   226 ------KRLQVLMKQITLRR 239
DEXDc smart00487
DEAD-like helicases superfamily;
723-912 4.38e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 4.38e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    723 TLKHYQLQGLEWMvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKrlNGPYLIIVPLSTL-SNWTYEFDKWAPS-V 799
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    800 VKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPR 875
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162

                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 212276472    876 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 912
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 724-949 8.21e-30

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 119.18  E-value: 8.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEW-----MVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHkrlnGPY---------LIIVPLSTLSNWT 789
Cdd:cd18066     1 LRPHQREGIEFlyecvMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQ----GPYggkpvikraLIVTPGSLVKNWK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  790 YEFDKWApsvvkisykGTPAMRRSLVPQ-------LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCK 862
Cdd:cd18066    77 KEFQKWL---------GSERIKVFTVDQdhkveefIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  863 LTQVLnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIR--RLHK 940
Cdd:cd18066   148 TTTAL-TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTR 226


                  ....*....
gi 212276472  941 VLRPFLLRR 949
Cdd:cd18066   227 LTGLFILRR 235
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 1383-1504 2.16e-29

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 113.55  E-value: 2.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1383 LTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYR 1462
Cdd:cd05515     1 MQQKLWELYNAVKNYTD------------------GRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQ 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 212276472 1463 SLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQ 1504
Cdd:cd05515    63 SLDDMVSDFVLMFDNACKYNEPDSQIYKDALTLQKVLLETKR 104
BROMO smart00297
bromo domain;
1381-1506 2.11e-28

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 110.45  E-value: 2.11e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   1381 PKLTKQMNAIIDTVINYKDRcnvekvpsnsqleiegnssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHK 1460
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--------------------HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGK 61

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 212276472   1461 YRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:smart00297   62 YSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 1050-1164 6.10e-28

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 109.22  E-value: 6.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  1050 GKFELLDRILPKLRatNHRVLLFCQMTSlmTIMEDYFAFR-NFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRA 1128
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 212276472  1129 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIG 1164
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 1383-1500 6.92e-27

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 106.27  E-value: 6.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1383 LTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYR 1462
Cdd:cd05519     1 LKAAMLEIYDAVLNCED------------------ETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYK 62

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 212276472 1463 SLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFK 1500
Cdd:cd05519    63 SLEEFLEDFHLMFANARTYNQEGSIVYEDAVEMEKAFK 100
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 724-937 9.71e-27

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 110.29  E-value: 9.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRLNgPYLIIVPLSTLSNWTYE 791
Cdd:cd18069     1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  792 FDKWAPSVVKISY--------------KGTPAMRRSLVPQLRsGKFNVLLTTYE-YIIKDKHILakirwkyMIVDEGHRM 856
Cdd:cd18069    77 FNKWLPPPEALPNvrprpfkvfilndeHKTTAARAKVIEDWV-KDGGVLLMGYEmFRLRPGPDV-------VICDEGHRI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  857 KNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIR 936
Cdd:cd18069   149 KNCHASTSQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCVDSTPQDVKLMRY 226


                  .
gi 212276472  937 R 937
Cdd:cd18069   227 R 227
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 724-949 1.56e-26

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 109.87  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWM----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLM----EHKRLNGPYLIIVPLSTLSNWTYEFDK 794
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  795 W-----APSVV--KISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL 867
Cdd:cd18067    81 WlggrlQPLAIdgGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  868 NThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLHK---VLRP 944
Cdd:cd18067   161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPI-LKGRDADASEKERQLGEEKLQElisIVNR 238


                  ....*
gi 212276472  945 FLLRR 949
Cdd:cd18067   239 CIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 724-937 3.45e-26

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 108.06  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSlynNNLNGILADEMGLGKTIQTIALITYLmehkRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:cd18010     1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLPPDD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  804 ----YKGTPAmrrslvpqLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHyvAPRR 876
Cdd:cd18010    74 iqviVKSKDG--------LRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRV 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVD-----LNEEETILI----IRR 937
Cdd:cd18010   144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYsgssnLEELHLLLLatimIRR 213
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 1421-1501 8.93e-26

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 102.84  E-value: 8.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1421 RQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFK 1500
Cdd:cd04369    17 RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGPGSPIYKDAKKLEKLFE 96


                  .
gi 212276472 1501 S 1501
Cdd:cd04369    97 K 97
HSA smart00573
domain in helicases and associated with SANT domains;
436-508 3.67e-24

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 97.47  E-value: 3.67e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276472    436 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 508
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 1417-1503 8.16e-24

Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99948  Cd Length: 103  Bit Score: 97.51  E-value: 8.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05517    17 DPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIK 96


                  ....*..
gi 212276472 1497 SVFKSAR 1503
Cdd:cd05517    97 KIFTAKK 103
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
 1259-1326 4.29e-22

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 91.17  E-value: 4.29e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472  1259 DRRREDARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1326
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HELICc smart00490
helicase superfamily c-terminal domain;
1081-1164 6.50e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.12  E-value: 6.50e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   1081 IMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRA 1160
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                    ....
gi 212276472   1161 HRIG 1164
Cdd:smart00490   79 GRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 724-949 1.44e-21

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 95.62  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHyQLQGLEWMVSLYNNNLNG-ILADEMGLGKTIQTIALI------------------TYLMEHKRLN----GPYLIIV 780
Cdd:cd18072     2 LLH-QKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALIlaqkntqnrkeeekekalTEWESKKDSTlvpsAGTLVVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  781 PLSTLSNWTYEFDKWAPS---VVKIsYKGtpAMRRSLVPQLRSgkFNVLLTTYEYIIKD---------KHILAKIRWKYM 848
Cdd:cd18072    81 PASLVHQWKNEVESRVASnklRVCL-YHG--PNRERIGEVLRD--YDIVITTYSLVAKEiptykeesrSSPLFRIAWARI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  849 IVDEGHRMKNHH-------CKLtqvlNTHYvaprRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG 921
Cdd:cd18072   156 ILDEAHNIKNPKvqasiavCKL----RAHA----RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG 227

                         250       260
                  ....*....|....*....|....*...
gi 212276472  922 ERvdLNeeetILIirrlhkvlRPFLLRR 949
Cdd:cd18072   228 ER--LN----ILT--------KSLLLRR 241
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 1419-1503 1.53e-21

Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 90.97  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1419 SGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSV 1498
Cdd:cd05518    19 SGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVYEDANILEKV 98


                  ....*
gi 212276472 1499 FKSAR 1503
Cdd:cd05518    99 LKEKR 103
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 1417-1506 1.72e-21

Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 91.24  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05524    19 SEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLW 98

                          90
                  ....*....|
gi 212276472 1497 SVFKSARQKI 1506
Cdd:cd05524    99 ELFLSARNEV 108
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 724-937 2.53e-21

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 94.95  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWM---------VSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNG--PYLIIVPLSTLSNWTYEF 792
Cdd:cd18068     1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  793 DKWAP--------SVVKISYKGTPAMRRsLVPQLRSGKFNVLLTTYE-YII----KDKHILAKIRWKYM----------- 848
Cdd:cd18068    81 EKWQEglkdeekiEVNELATYKRPQERS-YKLQRWQEEGGVMIIGYDmYRIlaqeRNVKSREKLKEIFNkalvdpgpdfv 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  849 IVDEGHRMKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGERVDLNE 928
Cdd:cd18068   160 VCDEGHILKNEASAVSKAMNS-IRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NGQCADSTL 237


                  ....*....
gi 212276472  929 EETILIIRR 937
Cdd:cd18068   238 VDVRVMKKR 246
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 1417-1501 3.31e-21

Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99951  Cd Length: 103  Bit Score: 90.09  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05520    17 NNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQ 96


                  ....*
gi 212276472 1497 SVFKS 1501
Cdd:cd05520    97 KLMQA 101
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
 437-503 5.90e-21

HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 88.01  E-value: 5.90e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212276472   437 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERM 503
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 746-903 3.85e-20

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 90.43  E-value: 3.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  746 ILADEMGLGKTIQTIALITYLM---EHKRLngpyLIIVPLSTLSNWTYE-FDKWAPSVVKISYKGTPAMRRSLVPQLRSg 821
Cdd:cd18011    21 LLADEVGLGKTIEAGLIIKELLlrgDAKRV----LILCPASLVEQWQDElQDKFGLPFLILDRETAAQLRRLIGNPFEE- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  822 kFNVLLTTYEYI---IKDKHILAKIRWKYMIVDEGHRMKNHHC-------KLTQVLNTHyvAPRRILLTGTPLQNKLPEL 891
Cdd:cd18011    96 -FPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEEDF 172

                         170
                  ....*....|..
gi 212276472  892 WALLNFLLPTIF 903
Cdd:cd18011   173 RALLSLLDPGRF 184
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1412-1492 5.49e-20

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 85.83  E-value: 5.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:pfam00439    2 LEILDKLMEHPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKA 81


                   .
gi 212276472  1492 S 1492
Cdd:pfam00439   82 A 82
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
 589-632 3.26e-16

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 462196  Cd Length: 44  Bit Score: 73.70  E-value: 3.26e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 212276472   589 QMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 632
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1417-1499 1.54e-15

Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 73.81  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05522    18 DENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLLE 97


                  ...
gi 212276472 1497 SVF 1499
Cdd:cd05522    98 KEA 100
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 724-898 4.16e-15

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 77.00  E-value: 4.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVslynnNLNGILADEMGLGKTIQTIALItylMEHKRLNGPY--------------------------- 776
Cdd:cd18070     1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALI---LLHPRPDNDLdaadddsdemvccpdclvaetpvsska 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  777 -LIIVPLSTLSNWTYEFDKWAPSVVKIS-YKG---TPAMRRSLVPQLRSgkFNVLLTTYEYIIKDKHI------------ 839
Cdd:cd18070    73 tLIVCPSAILAQWLDEINRHVPSSLKVLtYQGvkkDGALASPAPEILAE--YDIVVTTYDVLRTELHYaeanrsnrrrrr 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212276472  840 ----------LAKIRWKYMIVDEghrMKNHHCKLTQVLNTHYVAPR--RILLTGTPLQNKLPELWALLNFL 898
Cdd:cd18070   151 qkryeappspLVLVEWWRVCLDE---AQMVESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFL 218
BRK smart00592
domain in transcription and CHROMO domain helicases;
590-632 1.86e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 1.86e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 212276472    590 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 632
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPR 43
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1412-1501 4.49e-14

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 76.00  E-value: 4.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:COG5076   154 KKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVD 233

                          90
                  ....*....|
gi 212276472 1492 SIVLQSVFKS 1501
Cdd:COG5076   234 AKELEKYFLK 243
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1417-1497 1.90e-13

Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99952  Cd Length: 106  Bit Score: 68.12  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNhkYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05521    18 EENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNARLYNTKGSVIYKYALILE 95


                  .
gi 212276472 1497 S 1497
Cdd:cd05521    96 K 96
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 1427-1508 2.49e-13

Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99936  Cd Length: 115  Bit Score: 67.81  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1427 FIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05504    33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQRFFIKRCRKL 112


                  ..
gi 212276472 1507 AK 1508
Cdd:cd05504   113 GL 114
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 1427-1506 6.07e-13

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 66.42  E-value: 6.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1427 FIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05509    22 FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTEYYKCANKLEKFFWKKLKEL 101
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 724-914 6.56e-13

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 69.69  E-value: 6.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSlynNNLNGILADeMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSN-WTYEFDKW-APSVVK 801
Cdd:cd18013     1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWnHLRNLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  802 ISYK-GTPAMRRSLVpqlrSGKFNVLLTTYEyIIKDKHILAKIRWKY--MIVDEGHRMKNHHCKLTQVLNTH-YVAPRRI 877
Cdd:cd18013    76 VSVAvGTERQRSKAA----NTPADLYVINRE-NLKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 212276472  878 LLTGTPLQNKLPELWALLNFL--LPTIFKSCSTF-EQWFN 914
Cdd:cd18013   151 GLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 173-207 1.52e-12

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 462622  Cd Length: 35  Bit Score: 63.12  E-value: 1.52e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 212276472   173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
 1333-1419 2.96e-11

Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99926 [Multi-domain]  Cd Length: 114  Bit Score: 62.08  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1333 NLEEMEEEVRLKKRKRRrNVDKDPAKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDT-VINYKDRCNVEKVPSNSQ 1411
Cdd:cd05494     1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETgARDLEDLQIVQEDPADKQ 77


                  ....*...
gi 212276472 1412 LEIEGNSS 1419
Cdd:cd05494    78 IDDEGRRS 85
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 1431-1501 4.01e-11

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99931  Cd Length: 102  Bit Score: 61.15  E-value: 4.01e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212276472 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05499    30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFND 100
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 1435-1482 4.94e-10

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 58.52  E-value: 4.94e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 212276472 1435 ELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05528    32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
 172-206 6.26e-10

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 55.62  E-value: 6.26e-10
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 212276472    172 SPFSPVQLHQLRAQILAYK-MLARGQPLPETLQLAV 206
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 1430-1488 9.65e-10

Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99958  Cd Length: 128  Bit Score: 58.12  E-value: 9.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472 1430 LPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQI 1488
Cdd:cd05529    52 VDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEI 110
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 1434-1501 1.74e-09

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 56.23  E-value: 1.74e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212276472 1434 KELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05503    28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 1382-1504 1.90e-09

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 56.63  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05525     2 RLAQVLKEICDAIITYKD------------------SNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYY 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 212276472 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQ 1504
Cdd:cd05525    64 KTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQAKH 106
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 1421-1506 1.41e-08

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 54.22  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1421 RQLSEVFIQLPSR-------KELPEYYELIRKPVDFKKIKERIR----NHkYRSLGDLEKDVMLLCHNAQTFNLEGSQIY 1489
Cdd:cd05502    11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpkspQH-YSSPEEFVADVRLMFKNCYKFNEEDSEVA 89

                          90
                  ....*....|....*..
gi 212276472 1490 EDSIVLQSVFKSARQKI 1506
Cdd:cd05502    90 QAGKELELFFEEQLKEI 106
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
 1437-1482 2.30e-08

Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99945  Cd Length: 98  Bit Score: 53.18  E-value: 2.30e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 212276472 1437 PEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05513    32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYN 77
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 1431-1500 2.80e-08

Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99930  Cd Length: 102  Bit Score: 53.05  E-value: 2.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFK 1500
Cdd:cd05498    30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 1434-1507 3.15e-08

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 53.42  E-value: 3.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212276472 1434 KELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIyedSIVLQSVFKSARQKIA 1507
Cdd:cd05511    28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVY---TKKAKEMLELAEELLA 98
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 1425-1482 1.43e-07

Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99944  Cd Length: 98  Bit Score: 50.86  E-value: 1.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 212276472 1425 EVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05512    20 EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYN 77
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 1435-1507 1.96e-07

Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99929  Cd Length: 107  Bit Score: 50.88  E-value: 1.96e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276472 1435 ELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGsqiyeDSIVL--QSVFKSARQKIA 1507
Cdd:cd05497    36 NLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPG-----DDVVLmaQTLEKLFLQKLA 105
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 744-882 2.47e-07

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 51.64  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  744 NGILADEMGLGKTIQTIALITYLMEHKRlnGPYLIIVPLSTLSNWTYE-FDKWAPSVVKISYKgTPAMRRSLVPQLRSGK 822
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAErLRELFGPGIRVAVL-VGGSSAEEREKNKLGD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212276472  823 FNVLLTTYEYIIKDKHILAKI---RWKYMIVDEGHRM----KNHHCKLTQVLNTHYVAPRRILLTGT 882
Cdd:cd00046    80 ADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
723-883 6.58e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 50.75  E-value: 6.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   723 TLKHYQLQGLE-WMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVP-LSTLSNWTYEFDKWAPSVV 800
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   801 KIS--YKGtpamrRSLVPQLRSGKfnVLLTTYEYIIKD----KHILAKIRWKYMIVDEGHRM--KNHhcklTQVLNtHYV 872
Cdd:pfam04851   82 EIGeiISG-----DKKDESVDDNK--IVVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE-YFK 149

                          170
                   ....*....|.
gi 212276472   873 APRRILLTGTP 883
Cdd:pfam04851  150 PAFLLGLTATP 160
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 1431-1501 7.56e-07

Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99938  Cd Length: 99  Bit Score: 48.87  E-value: 7.56e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212276472 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05506    27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIFET 97
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1431-1501 9.91e-07

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 48.98  E-value: 9.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212276472 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05495    31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQ 101
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 46-450 1.05e-06

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: 53.62  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    46 PSPGPPSVSHPMPTmgstdfPQEGMHQMHKPidGIHdkgivedihcgSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPHP 125
Cdd:pfam03154  253 TQPPPPSQVSPQPL------PQPSLHGQMPP--MPH-----------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   126 SPLGApeHVSSPMSGGGPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSPV------QLHQLRAQILA---YKMLARGQ 196
Cdd:pfam03154  314 SPAAP--GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIpqlpnpQSHKHPPHLSGpspFQMNSNLP 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   197 PLPETLQLAvqgkrtlpglqqqqqqqqqqqqqqqqqqqqqqqpqqqppqpqtqqqqqpALVNYNRPSGPGPELSGPSTPQ 276
Cdd:pfam03154  392 PPPALKPLS-------------------------------------------------SLSTHHPPSAHPPPLQLMPQSQ 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   277 KLPVP---APGGRPSPAPPAAAQPPAAAVPGPSVP-QP-------APGQPSPVLQLQQKQSRISP----IQKPQG----- 336
Cdd:pfam03154  423 QLPPPpaqPPVLTQSQSLPPPAASHPPTSGLHQVPsQSpfpqhpfVPGGPPPITPPSGPPTSTSSampgIQPPSSasvss 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   337 -----------LDPVEILQEreyrlqariahRIQELENlPGSLPPDLR------TKATVELKALRLLNFQRQLRQEVVAC 399
Cdd:pfam03154  503 sgpvpaavscpLPPVQIKEE-----------ALDEAEE-PESPPPPPRspspepTVVNTPSHASQSARFYKHLDRGYNSC 570

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472   400 MRRDTTLETALNSK-------AYKRSKRQTLREARMTEKLEKQQKIEQERKR-RQKHQE 450
Cdd:pfam03154  571 ARTDLYFMPLAGSKlakkreeALEKAKREAEQKAREEKEREKEKEKEREREReREREAE 629
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 1431-1499 2.05e-06

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99932  Cd Length: 103  Bit Score: 47.69  E-value: 2.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVF 1499
Cdd:cd05500    31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 1424-1508 2.15e-06

Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99928  Cd Length: 119  Bit Score: 48.22  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNL-EGSQIYEDSIVLQSVFKSA 1502
Cdd:cd05496    23 SEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTPnKRSRIYSMTLRLSALFEEH 102


                  ....*.
gi 212276472 1503 RQKIAK 1508
Cdd:cd05496   103 IKKIIS 108
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 724-883 4.02e-06

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 48.07  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  724 LKHYQLQGLEWMVSLYNNNLnGILADEMGLGKTIQTIALITYLMEHKrlngpYLIIVP-LSTLSNWTYEFDKWAPSVVki 802
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRR-GILVLPTGSGKTLTALALIAYLKELR-----TLIVVPtDALLDQWKERFEDFLGDSS-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  803 sykgtpamrrslVPQLRSGK------FNVLLTTYEYIIKDKHILAKI--RWKYMIVDEGHrmknHHC--KLTQVLnTHYV 872
Cdd:cd17926    73 ------------IGLIGGGKkkdfddANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KELN 135

                         170
                  ....*....|.
gi 212276472  873 APRRILLTGTP 883
Cdd:cd17926   136 AKYRLGLTATP 146
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
 1424-1482 6.65e-06

Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99939  Cd Length: 104  Bit Score: 46.20  E-value: 6.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1424 SEVFIQ-LPSRKElPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05507    21 ASVFLKpVTEDIA-PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
721-883 1.73e-05

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 49.25  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  721 NGTLKHYQLQGLE-WMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLngpyLIIVPLSTLSN-WTYEFDKWAPS 798
Cdd:COG1061    78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  799 VVKISYKgtpamrrslvpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVA 873
Cdd:COG1061   154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPA 213

                         170
                  ....*....|
gi 212276472  874 PRRILLTGTP 883
Cdd:COG1061   214 AYRLGLTATP 223
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 44-164 1.82e-05

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 48.66  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    44 MGPSPGPPSVSHPMPTMGSTDFPQEGMHQMHKpidgihdkgivedihcgsmkGTGMRPPHPGmGPPQSPMDQHSQG---Y 120
Cdd:pfam15279  190 MEPSSMPPPFLRPPPSIPQPNSPLSNPMLPGI--------------------GPPPKPPRNL-GPPSNPMHRPPFSphhP 248

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 212276472   121 MSPHPSPLGAPEhvSSPMSGGGPTPPQMPPSQPGALIPGDPQAM 164
Cdd:pfam15279  249 PPPPTPPGPPPG--LPPPPPRGFTPPFGPPFPPVNMMPNPPEMN 290
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 1424-1482 2.09e-05

Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 45.12  E-value: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05510    26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
 1418-1508 2.25e-05

Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99956  Cd Length: 110  Bit Score: 45.05  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1418 SSGRQLSEVFIQLPSRKELPEyyELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQS 1497
Cdd:cd05526    21 EEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSEIYEDAVELQQ 98

                          90
                  ....*....|.
gi 212276472 1498 VFKSARQKIAK 1508
Cdd:cd05526    99 FFIKIRDELCK 109
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 1117-1165 4.41e-05

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 43.08  E-value: 4.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 212276472 1117 SQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQ 1165
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 340-551 4.75e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  340 VEILQEREYRLQARIA-------HRIQELEnlpgslppDLRTKATVELKALRLLNFQRQLRQEVVAcmRRDTTLETALNS 412
Cdd:COG1196   283 LEEAQAEEYELLAELArleqdiaRLEERRR--------ELEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEE 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  413 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQK 492
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 212276472  493 KETERIEKERMRRLMAEDEEGYRKLIDQKKDRRLAyLLQQTDEYVANLTNLVWEHKQAQ 551
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAA 490
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 752-883 4.77e-05

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 45.31  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   752 GLGKTIqtIALITYL-MEHKRLNGPY-LIIVPLSTLSNWTYE-FDKWAPSV---VKISYKGTPamRRSLVPQLRSGkfNV 825
Cdd:pfam00270   24 GSGKTL--AFLLPALeALDKLDNGPQaLVLAPTRELAEQIYEeLKKLGKGLglkVASLLGGDS--RKEQLEKLKGP--DI 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276472   826 LLTTYE---YIIKDKHILAKIrwKYMIVDEGHRM--KNHHCKLTQVLNTHYVAPRRILLTGTP 883
Cdd:pfam00270   98 LVGTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
PHA03378 PHA03378
EBNA-3B; Provisional
 66-382 5.96e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   66 PQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPMSGGGPTP 145
Cdd:PHA03378  529 PPQPRAGRRAPCVYTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWP 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  146 PQMPPSQPG-----ALIPgdpqAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGLQQQ 218
Cdd:PHA03378  599 VPHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPY 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  219 QQQQQQQQQQQQQQQQQQQQPQQQP--------PQPQTQQQQQPALVNYNRPSGPGPELSGPSTPQKLPVPAPGGRPSPA 290
Cdd:PHA03378  675 QPSPTGANTMLPIQWAPGTMQPPPRaptpmrppAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 754

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  291 PPAAAQPPAAAVPGPSVPQPAPGQP--SPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELENLPG 366
Cdd:PHA03378  755 RPPAAAPGRARPPAAAPGAPTPQPPpqAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGGVK 834

                         330
                  ....*....|....*.
gi 212276472  367 SLPPDLRTKATVELKA 382
Cdd:PHA03378  835 RGRPSLKKPAALERQA 850
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 45-162 6.59e-05

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 46.13  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    45 GPSPGPPSVSHPMPTM---GST-DFPQEGMH--QMHKPIDGIHDKGIVEDIHC-GSMK----GTGM-----------RP- 101
Cdd:pfam15822   88 GPSCPPPGGPYPAPTVpgpGPIgPYPTPNMPfpELPRPYGAPTDPAAAAPSGPwGSMSsgpwAPGMggqypapnmpyPSp 167

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212276472   102 -PHPGMGPPQSP----------MDQHSQGYMSPHPSPLGapehvSSPMSGGGPTPP---QMPPSQPGA-LIPGDPQ 162
Cdd:pfam15822  168 gPYPAVPPPQSPgaappvpwgtVPPGPWGPPAPYPDPTG-----SYPMPGLYPTPNnpfQVPSGPSGApPMPGGPH 238
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 1424-1488 1.33e-04

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 42.52  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276472 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQI 1488
Cdd:cd05505    18 SWPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYYENGSYV 82
Bromo_ZMYND11 cd05492
Bromodomain; ZMYND11_like sub-family. ZMYND11 or BS69 is a ubiquitously expressed nuclear ...
 1436-1490 1.43e-04

Bromodomain; ZMYND11_like sub-family. ZMYND11 or BS69 is a ubiquitously expressed nuclear protein that has been shown to associate with chromatin. It interacts with chromatin remodeling factors and might play a role in chromatin remodeling and gene expression. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99924  Cd Length: 109  Bit Score: 42.75  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 212276472 1436 LPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYE 1490
Cdd:cd05492    36 LPKRRRLIHTHLDVADIQEKINSEKYTSLEEFKADALLLLHNTAIFHGADSEQYD 90
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
 752-851 3.58e-04

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 43.47  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  752 GLGKTiqTIALITYLMEHKRlNGPYLIIVPLSTLSNWTYE----FDKWAPSVVKI--SYKGTPAMRR-SLVPQLRSGKFN 824
Cdd:cd17924    42 GVGKT--TFGLATSLYLASK-GKRSYLIFPTKSLVKQAYErlskYAEKAGVEVKIlvYHSRLKKKEKeELLEKIEKGDFD 118

                          90       100
                  ....*....|....*....|....*..
gi 212276472  825 VLLTTYEYIIKDKHILAKIRWKYMIVD 851
Cdd:cd17924   119 ILVTTNQFLSKNFDLLSNKKFDFVFVD 145
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 100-176 5.08e-04

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.72  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   100 RPPHPGMGPPQSPMDQHsqgymsPHPSPLGAPEHvsSPMSGG-----GPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPF 174
Cdd:pfam15240   48 GPPPGGFPPQPPASDDP------PGPPPPGGPQQ--PPPQGGkqkpqGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPG 119


                   ..
gi 212276472   175 SP 176
Cdd:pfam15240  120 KP 121
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
 1424-1506 9.57e-04

Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99940  Cd Length: 99  Bit Score: 40.06  E-value: 9.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSivlQSVFKSAR 1503
Cdd:cd05508    20 AEPFLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYNGGDHKLTQAA---KAIVKICE 96


                  ...
gi 212276472 1504 QKI 1506
Cdd:cd05508    97 QEM 99
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-525 1.25e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   333 KPQGLDPVEILQEREY-------RLQARIAHRIQELENLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTT 405
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   406 LETALnskAYKRSKRQTLRE--ARMTEKLEKQQKIEQERKRRQKHQEyLNSILQHAKDFKEYHRSVAGKIQKLskavatw 483
Cdd:TIGR02169  749 LEQEI---ENVKSELKELEAriEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSKLEEEVSRIEARLREI------- 817

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 212276472   484 hanterEQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRR 525
Cdd:TIGR02169  818 ------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 92-173 2.14e-03

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.79  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    92 GSMKGTGMRPPHPG--MGPPQSPMDQHSQGymsphPSPLGAPEhvSSPMSGGGPtPPQMPPSQPGALIPGDPQAMSQPNR 169
Cdd:pfam15240   58 PPASDDPPGPPPPGgpQQPPPQGGKQKPQG-----PPPQGGPR--PPPGKPQGP-PPQGGNQQQGPPPPGKPQGPPPQGG 129


                   ....
gi 212276472   170 GPSP 173
Cdd:pfam15240  130 GPPP 133
PTZ00121 PTZ00121
MAEBL; Provisional
 413-524 2.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  413 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHAntEREQK 492
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614

                          90       100       110
                  ....*....|....*....|....*....|..
gi 212276472  493 KETERIEKERMRRlmaedEEGYRKLIDQKKDR 524
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 43-170 2.67e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 41.95  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   43 MMGPSPGPPSVS-HPMPTMGSTDFPQEGMHQMHKPIDGIHdkgivEDIHCGSMKGTGMRPPHPGMGPPQSPmdQHSQGYM 121
Cdd:cd22056   195 MMAAGGGGFMGQqKPKHQMHSVHPQAFTHHQAAGPGALQG-----RGGRGGPDCHLLHSSHHHHHHHHLQY--QYMNAPY 267

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212276472  122 SPHPSPLGAP----------EHVS---SPMSGGGPTPPQMPPSQPgaLIPGDPQAMSQPNRG 170
Cdd:cd22056   268 PPHYAHQGAPqfhgqysvfrEPMRvhhQGHPGSMLTPPSSPPLLE--FYAQDEPEDIKPKRG 327
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 98-199 2.82e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.16  E-value: 2.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472     98 GMRPPH--PGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPMsgggptPPQMPPSQPGALIPGDPQAMSQPNrgpspfS 175
Cdd:smart00818   51 TLQPHHhiPVLPAQQPVVPQQPLMPVPGQHSMTPTQHHQPNLP------QPAQQPFQPQPLQPPQPQQPMQPQ------P 118

                            90       100
                    ....*....|....*....|....
gi 212276472    176 PVQLHQLRAQILAYKMLARGQPLP 199
Cdd:smart00818  119 PVHPIPPLPPQPPLPPMFPMQPLP 142
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 46-182 5.06e-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: 41.56  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472    46 PSPGPPSVSHPMPTMGSTDFPQEGMHQMHKPIDGIHDKGIVEDIHcgsmkgtgMRPPHPGMGPPQSPMDQHSQGYMSPHP 125
Cdd:pfam09770  222 PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTIL--------QRPQSPQPDPAQPSIQPQAQQFHQQPP 293

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276472   126 SPLGAPEH------VSSPMSGGGPTPPQmPPSQPGALIPGDPQAMSQPNRGPSPFSPVQLHQL 182
Cdd:pfam09770  294 PVPVQPTQilqnpnRLSAARVGYPQNPQ-PGVQPAPAHQAHRQQGSFGRQAPIITHPQQLAQL 355
PHA03247 PHA03247
large tegument protein UL36; Provisional
 45-315 5.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   45 GPSPG---------PPSVSHPMPTMGSTDFPQEGMH-QMHKPIDGIHDkgivedihCGSMKGTGMRPPHPGMGPPQSPmD 114
Cdd:PHA03247 2495 APDPGgggppdpdaPPAPSRLAPAILPDEPVGEPVHpRMLTWIRGLEE--------LASDDAGDPPPPLPPAAPPAAP-D 2565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  115 QHSqgymsPHPSPLGAPehvSSPMSGGGPTPPQMPPSQPGALIPGDPqamSQPNRGPSPFSPVQLHQLRAQILAYKMLAR 194
Cdd:PHA03247 2566 RSV-----PPPRPAPRP---SEPAVTSRARRPDAPPQSARPRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPA 2634

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472  195 GQPLPETLQLAVQgKRTLPGLQQQQQQQQQQQQQQQQQQQQQQQPQQQPPQPQTQQQQQPALVNYNRPSGPGPELSGPST 274
Cdd:PHA03247 2635 ANEPDPHPPPTVP-PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPH 2713

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 212276472  275 PQKLPVPAPGGrpspapPAAAQPPAAAVPGPSVPQPAPGQP 315
Cdd:PHA03247 2714 ALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGP 2748
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 315-535 6.26e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   315 PSPVLQLQQKQ----SRISPIQKPQGLDPVEILQEREYRL--QARIAHRIQELENlpgslppdlRTKATVELKALRLLNF 388
Cdd:pfam15709  280 LSSKYDAEESQvsidGRSSPTQTFVVTGNMESEEERSEEDpsKALLEKREQEKAS---------RDRLRAERAEMRRLEV 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276472   389 ---------QRQLRQEVvacMRRDTTLETALNSKAYKRSKRQTLREARMTEklEKQQKIEQERKRRQKHQEYLNSILQHA 459
Cdd:pfam15709  351 erkrreqeeQRRLQQEQ---LERAEKMREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQLQAAQERARQQQ 425

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212276472   460 KdfkEYHRSVAgKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMAEDEEgyrklidqkkdRRLAYLLQQTDE 535
Cdd:pfam15709  426 E---EFRRKLQ-ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-----------ERLEYQRQKQEA 486
 
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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