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Conserved domains on  [gi|51593084|ref|NP_035546|]
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probable global transcription activator SNF2L2 isoform 1 [Mus musculus]

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 ...
712-962 1.12e-174

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: 523.47  E-value: 1.12e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  712 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 791
Cdd:cd18063    1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  792 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 871
Cdd:cd18063   81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  872 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 951
Cdd:cd18063  161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
                        250
                 ....*....|.
gi 51593084  952 VLRPFLLRRLK 962
Cdd:cd18063  241 VLRPFLLRRLK 251
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
731-1213 1.04e-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: 525.91  E-value: 1.04e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   731 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 810
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   811 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 886
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   887 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 966
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   967 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1045
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  1046 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1125
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  1126 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1205
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                  ....*...
gi 51593084  1206 DQKVIQAG 1213
Cdd:PLN03142  616 DALVIQQG 623
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1393-1499 1.62e-62

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: 208.05  E-value: 1.62e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1393 KLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQ 1472
Cdd:cd05516    1 ELTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                         90       100
                 ....*....|....*....|....*..
gi 51593084 1473 TFNLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:cd05516   81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
HSA smart00573
domain in helicases and associated with SANT domains;
447-519 4.99e-24

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 97.08  E-value: 4.99e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084     447 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 519
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1270-1337 2.18e-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: 91.94  E-value: 2.18e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51593084   1270 DRRREDARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1337
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
600-643 3.09e-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: 3.09e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 51593084    600 QMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 643
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 2.13e-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: 62.74  E-value: 2.13e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 51593084    173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
PHA03378 super family cl33729
EBNA-3B; Provisional
74-393 3.67e-07

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.07  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    74 HKPMDG-------IHDKGIVEDVHCGSMKGTSMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPISGGGPTPP 146
Cdd:PHA03378  530 PQPRAGrrapcvyTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWPV 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   147 QMPPSQPG-----ALIPgdpqAMNQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGMQQQQ 219
Cdd:PHA03378  600 PHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPYQ 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   220 QQQQQQQQQQQQQQQQQQQQQQPQQPQQQAQAQPQQQQQQQQQPALVSYNRPSG-PGQELLLSGQSAPQKLSAPAPSGRP 298
Cdd:PHA03378  676 PSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAaPGRARPPAAAPGRARPPAAAPGRAR 755
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   299 SPAPQAAVQPTATAVPG-PSVQQPAPGQPSPvlqLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELESL 375
Cdd:PHA03378  756 PPAAAPGRARPPAAAPGaPTPQPPPQAPPAP---QQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGG 832
                         330
                  ....*....|....*...
gi 51593084   376 PGSLPPDLRTKATVELKA 393
Cdd:PHA03378  833 VKRGRPSLKKPAALERQA 850
Bromodomain super family cl02556
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1344-1439 6.99e-06

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: 46.67  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1344 NLEEMEEEVRLKKRKRRrNVDKDPVKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDTVInyKDSSGRQlsevfIQL 1423
Cdd:cd05494    1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETGA--RDLEDLQ-----IVQ 70
                         90
                 ....*....|....*.
gi 51593084 1424 PSRKDLPEYYELIRKP 1439
Cdd:cd05494   71 EDPADKQIDDEGRRSP 86
 
Name Accession Description Interval E-value
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
712-962 1.12e-174

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: 523.47  E-value: 1.12e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  712 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 791
Cdd:cd18063    1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  792 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 871
Cdd:cd18063   81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  872 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 951
Cdd:cd18063  161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
                        250
                 ....*....|.
gi 51593084  952 VLRPFLLRRLK 962
Cdd:cd18063  241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
731-1213 1.04e-164

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 525.91  E-value: 1.04e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   731 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 810
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   811 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 886
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   887 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 966
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   967 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1045
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  1046 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1125
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  1126 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1205
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                  ....*...
gi 51593084  1206 DQKVIQAG 1213
Cdd:PLN03142  616 DALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
731-1197 4.53e-122

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 398.83  E-value: 4.53e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  731 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 810
Cdd:COG0553  238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  811 VKISYKGTPAmRRSLVPQLRsgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRR 887
Cdd:COG0553  317 RVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHR 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  888 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtgervdlNEEETILIIRRLHKVLRPFLLRRLKKEVES 967
Cdd:COG0553  390 LALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----------IEKGDEEALERLRRLLRPFLLRRTKEDVLK 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  968 QLPEKVEYVIKCDMSALQKILYRHMQAKgillTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHlgys 1047
Cdd:COG0553  460 DLPEKTEETLYVELTPEQRALYEAVLEY----LRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR---- 531
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1048 ngvingaelyraSGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEpG 1127
Cdd:COG0553  532 ------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-G 598
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1128 SQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1197
Cdd:COG0553  599 PEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
738-1033 2.61e-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: 359.69  E-value: 2.61e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    738 YQLQGLEWMVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRLNGPYLIIVPLSTLSNWTYEFDKWA--PSVVKI 813
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    814 SYKGTP-AMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTG 892
Cdd:pfam00176   81 VLHGNKrPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    893 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetiLIIRRLHKVLRPFLLRRLKKEVESQLPEK 972
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51593084    973 VEYVIKCDMSALQKILY-RHMQAKGILLTDGSEkdkKGKGGAKTLMNTIMQLRKICNHPYMF 1033
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1393-1499 1.62e-62

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: 208.05  E-value: 1.62e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1393 KLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQ 1472
Cdd:cd05516    1 ELTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                         90       100
                 ....*....|....*....|....*..
gi 51593084 1473 TFNLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:cd05516   81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1060-1186 1.68e-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: 1.68e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1060 SGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPgSQYFIFLLSTRA 1139
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 51593084 1140 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1186
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
734-923 4.89e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 4.89e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     734 TLKHYQLQGLEWMvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKrlNGPYLIIVPLSTL-SNWTYEFDKWAPS-V 810
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     811 VKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPR 886
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 51593084     887 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 923
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
BROMO smart00297
bromo domain;
1392-1499 6.33e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 117.76  E-value: 6.33e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    1392 PKLTKQMNAIIDTVINYKDSsgRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNA 1471
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|....*...
gi 51593084    1472 QTFNLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1061-1175 5.15e-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: 109.61  E-value: 5.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   1061 GKFELLDRILPKLRatNHRVLLFCQMTSlmTIMEDYFAFR-NFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRA 1139
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 51593084   1140 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIG 1175
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HSA smart00573
domain in helicases and associated with SANT domains;
447-519 4.99e-24

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 97.08  E-value: 4.99e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084     447 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 519
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1270-1337 2.18e-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: 91.94  E-value: 2.18e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51593084   1270 DRRREDARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1337
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HELICc smart00490
helicase superfamily c-terminal domain;
1092-1175 5.54e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 5.54e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    1092 IMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRA 1171
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 51593084    1172 HRIG 1175
Cdd:smart00490   79 GRAG 82
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
448-514 7.07e-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: 87.63  E-value: 7.07e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51593084    448 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERM 514
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1398-1485 9.75e-19

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: 82.36  E-value: 9.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   1398 MNAIIDTVINykdssgRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLE 1477
Cdd:pfam00439    1 CLEILDKLME------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGP 74

                   ....*...
gi 51593084   1478 GSQIYEDS 1485
Cdd:pfam00439   75 GSVIYKAA 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1373-1494 3.03e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 82.55  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1373 EKAKKRRGRPPAEKLspnppKLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNH 1452
Cdd:COG5076  127 KTSVKKRKTPKIEDE-----LLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNG 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 51593084 1453 KYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1494
Cdd:COG5076  202 RYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLK 243
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
600-643 3.09e-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: 3.09e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 51593084    600 QMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 643
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
601-643 1.73e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 1.73e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51593084     601 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 643
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPR 43
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-207 2.13e-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: 62.74  E-value: 2.13e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 51593084    173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
172-206 8.60e-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: 55.23  E-value: 8.60e-10
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 51593084     172 SPFSPVQLHQLRAQILAYK-MLARGQPLPETLQLAV 206
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
PHA03378 PHA03378
EBNA-3B; Provisional
74-393 3.67e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.07  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    74 HKPMDG-------IHDKGIVEDVHCGSMKGTSMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPISGGGPTPP 146
Cdd:PHA03378  530 PQPRAGrrapcvyTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWPV 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   147 QMPPSQPG-----ALIPgdpqAMNQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGMQQQQ 219
Cdd:PHA03378  600 PHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPYQ 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   220 QQQQQQQQQQQQQQQQQQQQQQPQQPQQQAQAQPQQQQQQQQQPALVSYNRPSG-PGQELLLSGQSAPQKLSAPAPSGRP 298
Cdd:PHA03378  676 PSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAaPGRARPPAAAPGRARPPAAAPGRAR 755
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   299 SPAPQAAVQPTATAVPG-PSVQQPAPGQPSPvlqLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELESL 375
Cdd:PHA03378  756 PPAAAPGRARPPAAAPGaPTPQPPPQAPPAP---QQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGG 832
                         330
                  ....*....|....*...
gi 51593084   376 PGSLPPDLRTKATVELKA 393
Cdd:PHA03378  833 VKRGRPSLKKPAALERQA 850
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1344-1439 6.99e-06

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: 46.67  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1344 NLEEMEEEVRLKKRKRRrNVDKDPVKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDTVInyKDSSGRQlsevfIQL 1423
Cdd:cd05494    1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETGA--RDLEDLQ-----IVQ 70
                         90
                 ....*....|....*.
gi 51593084 1424 PSRKDLPEYYELIRKP 1439
Cdd:cd05494   71 EDPADKQIDDEGRRSP 86
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
732-894 1.80e-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: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  732 NGTLKHYQLQGLE-WMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLngpyLIIVPLSTLSN-WTYEFDKWAPS 809
Cdd:COG1061   78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  810 VVKISYKgtpamrrslvpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVA 884
Cdd:COG1061  154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPA 213
                        170
                 ....*....|
gi 51593084  885 PRRILLTGTP 894
Cdd:COG1061  214 AYRLGLTATP 223
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
22-461 2.36e-05

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: 49.38  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     22 SPGPILGPSPGPGPSPGSVHSMMGPSP-----GPPSVSHPLSTMGSADFPQEGMHQLHKPmdgihdKGIVEDVHCGSMKG 96
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQPSLHGQMPPMPhslqtGPSHMQHPVPPQPFPLTPQSSQSQVPPG------PSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     97 TSmrPPHPGMGPPQSPMDQ------HSQGYMSPHP----SPLGAPEHVSSPISGGGPTPPQMPPS--QPGALIPGDPQAM 164
Cdd:pfam03154  327 TP--PSQSQLQSQQPPREQplppapLSMPHIKPPPttpiPQLPNPQSHKHPPHLSGPSPFQMNSNlpPPPALKPLSSLST 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    165 NQPNRGPSPfsPVQLhqlraqilaykmLARGQPLPETlqlAVQGkrtlPGMQQQQQqqqqqqqqqqqqqqqqqqqqqpqq 244
Cdd:pfam03154  405 HHPPSAHPP--PLQL------------MPQSQQLPPP---PAQP----PVLTQSQS------------------------ 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    245 pqqqaqaqpqqqqqqqqqpalVSYNRPSGPGQELLLSGQSAPQKLSAPAPSGRPSPAPQAAVQPTATAVPGPSVQQPAPG 324
Cdd:pfam03154  440 ---------------------LPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    325 QPSPVLQLQQKQSRISPiqkpqgldPVEILQEreyrlqariahRIQELESlPGSLPPDLR------TKATVELKALRLLN 398
Cdd:pfam03154  499 SVSSSGPVPAAVSCPLP--------PVQIKEE-----------ALDEAEE-PESPPPPPRspspepTVVNTPSHASQSAR 558
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51593084    399 FQRQLRQEVVACMRRDTTLETALNSK-------AYKRSKRQTLREARMTEKLEKQQKIEQERKR-RQKHQE 461
Cdd:pfam03154  559 FYKHLDRGYNSCARTDLYFMPLAGSKlakkreeALEKAKREAEQKAREEKEREKEKEKEREREReREREAE 629
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
344-536 5.18e-04

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: 45.06  E-value: 5.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    344 KPQGLDPVEILQEREY-------RLQARIAHRIQELESLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTT 416
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    417 LETALnskAYKRSKRQTLRE--ARMTEKLEKQQKIEQERKRRQKHQEyLNSILQHAKDFKEYHRSVAGKIQKLskavatw 494
Cdd:TIGR02169  749 LEQEI---ENVKSELKELEAriEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSKLEEEVSRIEARLREI------- 817
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 51593084    495 hanterEQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRR 536
Cdd:TIGR02169  818 ------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
PTZ00121 PTZ00121
MAEBL; Provisional
424-535 1.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   424 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHAntEREQK 503
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                          90       100       110
                  ....*....|....*....|....*....|..
gi 51593084   504 KETERIEKERMRRlmaedEEGYRKLIDQKKDR 535
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
 
Name Accession Description Interval E-value
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
712-962 1.12e-174

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: 523.47  E-value: 1.12e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  712 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 791
Cdd:cd18063    1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  792 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 871
Cdd:cd18063   81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  872 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 951
Cdd:cd18063  161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
                        250
                 ....*....|.
gi 51593084  952 VLRPFLLRRLK 962
Cdd:cd18063  241 VLRPFLLRRLK 251
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
732-962 9.59e-170

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: 509.60  E-value: 9.59e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  732 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVV 811
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  812 KISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLT 891
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084  892 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERV--DLNEEETILIIRRLHKVLRPFLLRRLK 962
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
731-1213 1.04e-164

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 525.91  E-value: 1.04e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   731 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 810
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   811 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 886
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   887 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 966
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   967 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1045
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  1046 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1125
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  1126 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1205
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                  ....*...
gi 51593084  1206 DQKVIQAG 1213
Cdd:PLN03142  616 DALVIQQG 623
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
712-962 3.97e-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: 490.33  E-value: 3.97e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  712 YYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 791
Cdd:cd18062    1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  792 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 871
Cdd:cd18062   81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  872 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 951
Cdd:cd18062  161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                        250
                 ....*....|.
gi 51593084  952 VLRPFLLRRLK 962
Cdd:cd18062  241 VLRPFLLRRLK 251
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
731-1197 4.53e-122

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 398.83  E-value: 4.53e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  731 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 810
Cdd:COG0553  238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  811 VKISYKGTPAmRRSLVPQLRsgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRR 887
Cdd:COG0553  317 RVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHR 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  888 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtgervdlNEEETILIIRRLHKVLRPFLLRRLKKEVES 967
Cdd:COG0553  390 LALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----------IEKGDEEALERLRRLLRPFLLRRTKEDVLK 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  968 QLPEKVEYVIKCDMSALQKILYRHMQAKgillTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHlgys 1047
Cdd:COG0553  460 DLPEKTEETLYVELTPEQRALYEAVLEY----LRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR---- 531
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1048 ngvingaelyraSGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEpG 1127
Cdd:COG0553  532 ------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-G 598
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1128 SQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1197
Cdd:COG0553  599 PEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
738-1033 2.61e-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: 359.69  E-value: 2.61e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    738 YQLQGLEWMVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRLNGPYLIIVPLSTLSNWTYEFDKWA--PSVVKI 813
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    814 SYKGTP-AMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTG 892
Cdd:pfam00176   81 VLHGNKrPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    893 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetiLIIRRLHKVLRPFLLRRLKKEVESQLPEK 972
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51593084    973 VEYVIKCDMSALQKILY-RHMQAKGILLTDGSEkdkKGKGGAKTLMNTIMQLRKICNHPYMF 1033
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 ...
732-962 3.96e-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: 298.15  E-value: 3.96e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  732 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrLNGPYLIIVPLSTLSNWTYEFDKWAPSVV 811
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  812 KISYKGTPAMRRSLVPQLRS-----GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPR 886
Cdd:cd18009   80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51593084  887 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN--APFAMTGERVDLNEEETILIIRRLHKVLRPFLLRRLK 962
Cdd:cd18009  159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
732-962 2.32e-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: 292.30  E-value: 2.32e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  732 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVV 811
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  812 KISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvaprR 887
Cdd:cd17997   81 VVVLIGDKEERADIIrDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVrlfNSRN----R 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51593084  888 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamTGERVDLNEEetilIIRRLHKVLRPFLLRRLK 962
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 ...
735-960 1.68e-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: 1.68e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRslvpQLRSG-----KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRIL 889
Cdd:cd18003   81 YYGSAKERK----LKRQGwmkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51593084  890 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF-AMTGERVDLNEEetilIIRRLHKVLRPFLLRR 960
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 ...
734-960 3.04e-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: 260.75  E-value: 3.04e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  734 TLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKI 813
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  814 SYKGTPAMRRSL------VPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRR 887
Cdd:cd17993   81 VYLGDIKSRDTIreyefyFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084  888 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgerVDLNEEETILiIRRLHKVLRPFLLRR 960
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 ...
735-911 3.72e-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: 3.72e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYvAPRRILLTGTP 894
Cdd:cd17919   81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159
                        170
                 ....*....|....*..
gi 51593084  895 LQNKLPELWALLNFLLP 911
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; ...
735-960 4.35e-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: 243.31  E-value: 4.35e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVkIS 814
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMNV-VV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRR-----------SLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 882
Cdd:cd17995   80 YHGSGESRQiiqqyemyfkdAQGRKKKGvYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51593084  883 VAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 960
Cdd:cd17995  159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
722-972 2.94e-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: 236.10  E-value: 2.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  722 RVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 801
Cdd:cd18064    3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  802 EFDKWAPSVVKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 880
Cdd:cd18064   83 EFKRWVPTLRAVCLIGDKDQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  881 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 960
Cdd:cd18064  162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRR 231
                        250
                 ....*....|..
gi 51593084  961 LKKEVESQLPEK 972
Cdd:cd18064  232 IKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
722-962 7.15e-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: 234.53  E-value: 7.15e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  722 RVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 801
Cdd:cd18065    3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  802 EFDKWAPSVVKISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 880
Cdd:cd18065   83 EFKRWVPSLRAVCLIGDKDARAAFIrDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  881 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 960
Cdd:cd18065  162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 231

                 ..
gi 51593084  961 LK 962
Cdd:cd18065  232 IK 233
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1393-1499 1.62e-62

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: 208.05  E-value: 1.62e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1393 KLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQ 1472
Cdd:cd05516    1 ELTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                         90       100
                 ....*....|....*....|....*..
gi 51593084 1473 TFNLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:cd05516   81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
735-960 2.69e-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: 212.36  E-value: 2.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLVP-------QLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRR 887
Cdd:cd18002   81 YWGNPKDRKVLRKfwdrknlYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51593084  888 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERV-DLNEEEtiliIRRLHKVLRPFLLRR 960
Cdd:cd18002  160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKtGLNEHQ----LKRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
735-960 2.73e-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: 2.73e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18054   21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRI 888
Cdd:cd18054  101 YIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51593084  889 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGERVDLNEEEtiliirrLHKVLRPFLLRR 960
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 ...
731-962 7.44e-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: 210.88  E-value: 7.44e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  731 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 810
Cdd:cd18012    1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  811 VKISYKGTPAMRRSLVpqlRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHYvaprR 887
Cdd:cd18012   80 KVLVIHGTKRKREKLR---ALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLKADH----R 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51593084  888 ILLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGERvDLNEEEtiliIRRLHKVLRPFLLRRLK 962
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, ...
735-960 4.26e-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: 205.75  E-value: 4.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVaPRRILLTGT 893
Cdd:cd18006   81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51593084  894 PLQNKLPELWALLNFLLPTIFkSCSTFEQWFNApFAMTGERVDLNEEetiliirrLHKVLRPFLLRR 960
Cdd:cd18006  160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1060-1186 1.68e-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: 1.68e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1060 SGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPgSQYFIFLLSTRA 1139
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 51593084 1140 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1186
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; ...
735-960 8.17e-56

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: 192.65  E-value: 8.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTpamrrslvpqlrsgkfNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRILLTGTP 894
Cdd:cd17994   81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51593084  895 LQNKLPELWALLNFLLPTIFKSCSTFeqwfnapfamTGERVDLNEEETiliIRRLHKVLRPFLLRR 960
Cdd:cd17994  144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
735-914 2.36e-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: 185.28  E-value: 2.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRlNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLVPQLRSG--KFNVLLTTYEYII---KDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRIL 889
Cdd:cd17998   80 YYGSQEERKHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INANFRLL 158
                        170       180
                 ....*....|....*....|....*
gi 51593084  890 LTGTPLQNKLPELWALLNFLLPTIF 914
Cdd:cd17998  159 LTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
738-911 1.80e-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: 1.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  738 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAP--------- 808
Cdd:cd18000    4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvvlhs 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  809 ---SVVKISYKGTPAMRRSLVPQLRsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNThy 882
Cdd:cd18000   84 sgsGTGSEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLRT-- 160
                        170       180
                 ....*....|....*....|....*....
gi 51593084  883 vaPRRILLTGTPLQNKLPELWALLNFLLP 911
Cdd:cd18000  161 --PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
735-960 7.57e-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: 177.16  E-value: 7.57e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18053   21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRI 888
Cdd:cd18053  101 YLGDINSRNMIRthewmhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51593084  889 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGERVDLNEEEtiliirrLHKVLRPFLLRR 960
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 ...
735-960 6.16e-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: 174.08  E-value: 6.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKR------LNGPYLIIVPLSTLSNWTYEFDKWAP 808
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  809 SVVK--ISYKGTPAMRRSLVPQLrsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPR 886
Cdd:cd17999   80 NAFLkpLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51593084  887 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT--GERVDLNEEETILIIRRLHKVLRPFLLRR 960
Cdd:cd17999  157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASrdSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
735-960 2.96e-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: 2.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT-----------------YLMEHKRLN---GPYLIIVPLS 794
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrennrpRFKKKPPASsakKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  795 TLSNWTYEFDKWAPSVVKISYKGTPAMrrSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 874
Cdd:cd18005   81 VLYNWKDELDTWGHFEVGVYHGSRKDD--ELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  875 TQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF----AMTGERVDLNEEETilIIRRLH 950
Cdd:cd18005  159 TQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK--RKQELA 235
                        250
                 ....*....|
gi 51593084  951 KVLRPFLLRR 960
Cdd:cd18005  236 VKLSKFFLRR 245
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
735-960 4.40e-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: 171.38  E-value: 4.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVkIS 814
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWTEMNA-IV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTpAMRRSLVPQLR-----------SG--KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTH 881
Cdd:cd18058   79 YHGS-QISRQMIQQYEmyyrdeqgnplSGifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLM 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51593084  882 YVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 960
Cdd:cd18058  158 ALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
735-960 1.56e-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: 170.25  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLVPQ--------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 874
Cdd:cd18057   81 YTGDKESRSVIRENefsfednaIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  875 TQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgerVDLNEEETiliIRRLHKVLR 954
Cdd:cd18057  161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                 ....*.
gi 51593084  955 PFLLRR 960
Cdd:cd18057  227 PHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
735-960 1.18e-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: 167.15  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRLNGPYLIIVPLSTLSNWTYEFDKWApSVVKIS 814
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQE-VYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRR--------------SLVPQlrSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 880
Cdd:cd18060   79 YHGSLASRQmiqqyemyckdsrgRLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  881 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 960
Cdd:cd18060  156 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
735-960 1.33e-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: 167.50  E-value: 1.33e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAmRRSLVPQ---------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCK 873
Cdd:cd18055   81 YTGDKD-SRAIIREnefsfddnaVKGGkkafkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  874 LTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgerVDLNEEETiliIRRLHKVL 953
Cdd:cd18055  160 FFRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLL 225

                 ....*..
gi 51593084  954 RPFLLRR 960
Cdd:cd18055  226 GPHMLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
738-960 2.08e-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: 166.78  E-value: 2.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  738 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPyLIIVPLSTLSNWTYEFDKWAPSV-VKISYK 816
Cdd:cd18001    4 HQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLrVKVFHG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  817 GTPAMRRSlvpQLRS--GKFNVLLTTYEYIIKDKHILA-----KIRWKYMIVDEGHRMKNHHCKLTQVLntHYV-APRRI 888
Cdd:cd18001   83 TSKKERER---NLERiqRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAKNRI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  889 LLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPF-------AMTGERVDLNEeetilIIRRLHKVLRPFLLRR 960
Cdd:cd18001  158 ILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPItrgrdkdATQGEKALGSE-----VAENLRQIIKPYFLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
735-960 1.17e-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: 164.43  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVkIS 814
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV-VV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMRRSLV--------PQLR----SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHY 882
Cdd:cd18059   79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51593084  883 VApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 960
Cdd:cd18059  159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
735-960 3.01e-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: 3.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 YKGTPAMR--------------------RSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 874
Cdd:cd18056   81 YVGDKDSRaiirenefsfednairggkkASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  875 TQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgerVDLNEEETiliIRRLHKVLR 954
Cdd:cd18056  161 FRVLNG-YSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDMLG 226

                 ....*.
gi 51593084  955 PFLLRR 960
Cdd:cd18056  227 PHMLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
735-960 4.99e-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: 4.99e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVS--LYNNNLNG---ILADEMGLGKTIQTIALITYLMEHKRLNGP----YLIIVPLSTLSNWTYEFDK 805
Cdd:cd18004    1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  806 W----APSVVKISYKGTPAMRRSLvpQLRSGK-FNVLLTTYE-YIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 879
Cdd:cd18004   81 WlglrRIKVVTADGNAKDVKASLD--FFSSAStYPVLIISYEtLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  880 ThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvDLNEEETILIIRRLH---KVLRPF 956
Cdd:cd18004  159 S-LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRF 236

                 ....
gi 51593084  957 LLRR 960
Cdd:cd18004  237 ILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
735-960 1.74e-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: 155.91  E-value: 1.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLynnnlNGILADEMGLGKTIQTIALI------------TYLMEHKRLNGPY-----LIIVPLSTLS 797
Cdd:cd18008    1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeELEENSSDPKKLYlskttLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  798 NWTYEFDK----WAPSVVKisYKGtpAMRRSLVPQLRSgkFNVLLTTY-----EY-----------IIKDKHILAKIRWK 857
Cdd:cd18008   76 QWKDEIEKhtkpGSLKVYV--YHG--SKRIKSIEELSD--YDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  858 YMIVDEGHRMKNHHCKLTQV---LNTHyvapRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFamtger 934
Cdd:cd18008  150 RVILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF------ 219
                        250       260
                 ....*....|....*....|....*.
gi 51593084  935 vdlnEEETILIIRRLHKVLRPFLLRR 960
Cdd:cd18008  220 ----SKNDRKALERLQALLKPILLRR 241
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
735-960 1.72e-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: 152.47  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTialITYLMEHKR--LNGPYLIIVPLSTLSNWTYEFDKWAPSVVk 812
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS---ITFLYEILLtgIRGPFLIIAPLSTIANWEREFRTWTDLNV- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  813 ISYKGTpAMRRSLVPQLR-------------SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 879
Cdd:cd18061   77 VVYHGS-LISRQMIQQYEmyfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  880 THYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLR 959
Cdd:cd18061  156 LMNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLR 221

                 .
gi 51593084  960 R 960
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 ...
735-927 1.14e-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: 1.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWM----VSLYNNNLNG---ILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWA 807
Cdd:cd18007    1 LKPHQVEGVRFLwsnlVGTDVGSDEGggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  808 PSVVkISYKGTPAMRRSLVPQLRSGKFN-------VLLTTYEY---IIKDKHILAKIRWKYM-----------IVDEGHR 866
Cdd:cd18007   81 PPDL-RPLLVLVSLSASKRADARLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEGHR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51593084  867 MKNHHCKLTQVLNTHYvAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAP 927
Cdd:cd18007  160 LKNEKSQLSKALSKVK-TKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKP 219
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1394-1497 4.39e-33

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: 123.95  E-value: 4.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1394 LTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQT 1473
Cdd:cd05515    1 MQQKLWELYNAVKNYTDGRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACK 80
                         90       100
                 ....*....|....*....|....
gi 51593084 1474 FNLEGSQIYEDSIVLQSVFKSARQ 1497
Cdd:cd05515   81 YNEPDSQIYKDALTLQKVLLETKR 104
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
738-960 1.54e-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: 127.20  E-value: 1.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  738 YQLQGLEWMVSLYNNNL-----------------------------NGILADEMGLGKTIQTIALItylmehkrLNGPYL 788
Cdd:cd18071    4 HQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LANFTL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  789 IIVPLSTLSNWTYEF-DKWAPSVVKI-SYKGTpamRRSLVPQLRSGKfNVLLTTY-----EYIIKDKHILAKIRWKYMIV 861
Cdd:cd18071   76 IVCPLSVLSNWETQFeEHVKPGQLKVyTYHGG---ERNRDPKLLSKY-DIVLTTYntlasDFGAKGDSPLHTINWLRVVL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  862 DEGHRMKNHHCKLTQ-VLNTHyvAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLnee 940
Cdd:cd18071  152 DEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTGL--- 225
                        250       260
                 ....*....|....*....|
gi 51593084  941 etiliiRRLHKVLRPFLLRR 960
Cdd:cd18071  226 ------KRLQVLMKQITLRR 239
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1394-1493 2.57e-31

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: 118.60  E-value: 2.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1394 LTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQT 1473
Cdd:cd05519    1 LKAAMLEIYDAVLNCEDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANART 80
                         90       100
                 ....*....|....*....|
gi 51593084 1474 FNLEGSQIYEDSIVLQSVFK 1493
Cdd:cd05519   81 YNQEGSIVYEDAVEMEKAFK 100
DEXDc smart00487
DEAD-like helicases superfamily;
734-923 4.89e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 4.89e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     734 TLKHYQLQGLEWMvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKrlNGPYLIIVPLSTL-SNWTYEFDKWAPS-V 810
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     811 VKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPR 886
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 51593084     887 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 923
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
BROMO smart00297
bromo domain;
1392-1499 6.33e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 117.76  E-value: 6.33e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    1392 PKLTKQMNAIIDTVINYKDSsgRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNA 1471
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|....*...
gi 51593084    1472 QTFNLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFFEKKLREL 107
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
735-960 8.01e-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: 8.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEW-----MVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHkrlnGPY---------LIIVPLSTLSNWT 800
Cdd:cd18066    1 LRPHQREGIEFlyecvMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQ----GPYggkpvikraLIVTPGSLVKNWK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  801 YEFDKWApsvvkisykGTPAMRRSLVPQ-------LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCK 873
Cdd:cd18066   77 KEFQKWL---------GSERIKVFTVDQdhkveefIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  874 LTQVLnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIR--RLHK 951
Cdd:cd18066  148 TTTAL-TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTR 226

                 ....*....
gi 51593084  952 VLRPFLLRR 960
Cdd:cd18066  227 LTGLFILRR 235
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1061-1175 5.15e-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: 109.61  E-value: 5.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   1061 GKFELLDRILPKLRatNHRVLLFCQMTSlmTIMEDYFAFR-NFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRA 1139
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 51593084   1140 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIG 1175
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1394-1494 2.72e-27

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: 107.07  E-value: 2.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1394 LTKQMNAIIDTVINYKdssgRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQT 1473
Cdd:cd04369    1 LKKKLRSLLDALKKLK----RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKT 76
                         90       100
                 ....*....|....*....|.
gi 51593084 1474 FNLEGSQIYEDSIVLQSVFKS 1494
Cdd:cd04369   77 YNGPGSPIYKDAKKLEKLFEK 97
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
735-948 8.37e-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: 8.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRLNgPYLIIVPLSTLSNWTYE 802
Cdd:cd18069    1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  803 FDKWAPSVVKISY--------------KGTPAMRRSLVPQLRsGKFNVLLTTYE-YIIKDKHILakirwkyMIVDEGHRM 867
Cdd:cd18069   77 FNKWLPPPEALPNvrprpfkvfilndeHKTTAARAKVIEDWV-KDGGVLLMGYEmFRLRPGPDV-------VICDEGHRI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  868 KNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIR 947
Cdd:cd18069  149 KNCHASTSQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCVDSTPQDVKLMRY 226

                 .
gi 51593084  948 R 948
Cdd:cd18069  227 R 227
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
735-960 1.10e-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: 110.64  E-value: 1.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWM----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLM----EHKRLNGPYLIIVPLSTLSNWTYEFDK 805
Cdd:cd18067    1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  806 W-----APSVV--KISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL 878
Cdd:cd18067   81 WlggrlQPLAIdgGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  879 NThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLHK---VLRP 955
Cdd:cd18067  161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPI-LKGRDADASEKERQLGEEKLQElisIVNR 238

                 ....*
gi 51593084  956 FLLRR 960
Cdd:cd18067  239 CIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
735-948 4.25e-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: 107.68  E-value: 4.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSlynNNLNGILADEMGLGKTIQTIALITYLmehkRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 814
Cdd:cd18010    1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLPPDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  815 ----YKGTPAmrrslvpqLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHyvAPRR 887
Cdd:cd18010   74 iqviVKSKDG--------LRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRV 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  888 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVD-----LNEEETILI----IRR 948
Cdd:cd18010  144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYsgssnLEELHLLLLatimIRR 213
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1396-1496 1.76e-25

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: 102.14  E-value: 1.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1396 KQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1475
Cdd:cd05518    3 KRMLALFLYVLEYREGSGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYN 82
                         90       100
                 ....*....|....*....|.
gi 51593084 1476 LEGSQIYEDSIVLQSVFKSAR 1496
Cdd:cd05518   83 EEGSQVYEDANILEKVLKEKR 103
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1395-1499 3.86e-25

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: 101.64  E-value: 3.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1395 TKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTF 1474
Cdd:cd05524    4 IAVCQELYDTIRNYKSEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAY 83
                         90       100
                 ....*....|....*....|....*
gi 51593084 1475 NLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:cd05524   84 YKPDSPEHKDACKLWELFLSARNEV 108
HSA smart00573
domain in helicases and associated with SANT domains;
447-519 4.99e-24

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 97.08  E-value: 4.99e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084     447 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 519
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1405-1496 1.05e-23

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: 97.12  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1405 VINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1484
Cdd:cd05517   12 VMTATDPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKD 91
                         90
                 ....*....|..
gi 51593084 1485 SIVLQSVFKSAR 1496
Cdd:cd05517   92 ANAIKKIFTAKK 103
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1270-1337 2.18e-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: 91.94  E-value: 2.18e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51593084   1270 DRRREDARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1337
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1388-1494 2.44e-22

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: 93.17  E-value: 2.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1388 SPNPpkltkqMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLL 1467
Cdd:cd05520    1 SSNP------LWQLYDTIRNARNNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLM 74
                         90       100
                 ....*....|....*....|....*..
gi 51593084 1468 CHNAQTFNLEGSQIYEDSIVLQSVFKS 1494
Cdd:cd05520   75 FENAKRYNVPNSRIYKDAEKLQKLMQA 101
HELICc smart00490
helicase superfamily c-terminal domain;
1092-1175 5.54e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 5.54e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    1092 IMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRA 1171
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 51593084    1172 HRIG 1175
Cdd:smart00490   79 GRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
735-960 1.53e-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: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHyQLQGLEWMVSLYNNNLNG-ILADEMGLGKTIQTIALI------------------TYLMEHKRLN----GPYLIIV 791
Cdd:cd18072    2 LLH-QKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALIlaqkntqnrkeeekekalTEWESKKDSTlvpsAGTLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  792 PLSTLSNWTYEFDKWAPS---VVKIsYKGtpAMRRSLVPQLRSgkFNVLLTTYEYIIKD---------KHILAKIRWKYM 859
Cdd:cd18072   81 PASLVHQWKNEVESRVASnklRVCL-YHG--PNRERIGEVLRD--YDIVITTYSLVAKEiptykeesrSSPLFRIAWARI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  860 IVDEGHRMKNHH-------CKLtqvlNTHYvaprRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG 932
Cdd:cd18072  156 ILDEAHNIKNPKvqasiavCKL----RAHA----RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG 227
                        250       260
                 ....*....|....*....|....*...
gi 51593084  933 ERvdLNeeetILIirrlhkvlRPFLLRR 960
Cdd:cd18072  228 ER--LN----ILT--------KSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
735-948 2.22e-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: 95.34  E-value: 2.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWM---------VSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNG--PYLIIVPLSTLSNWTYEF 803
Cdd:cd18068    1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  804 DKWAP--------SVVKISYKGTPAMRRsLVPQLRSGKFNVLLTTYE-YII----KDKHILAKIRWKYM----------- 859
Cdd:cd18068   81 EKWQEglkdeekiEVNELATYKRPQERS-YKLQRWQEEGGVMIIGYDmYRIlaqeRNVKSREKLKEIFNkalvdpgpdfv 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  860 IVDEGHRMKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGERVDLNE 939
Cdd:cd18068  160 VCDEGHILKNEASAVSKAMNS-IRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NGQCADSTL 237

                 ....*....
gi 51593084  940 EETILIIRR 948
Cdd:cd18068  238 VDVRVMKKR 246
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
448-514 7.07e-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: 87.63  E-value: 7.07e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51593084    448 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERM 514
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
757-914 4.02e-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: 4.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  757 ILADEMGLGKTIQTIALITYLM---EHKRLngpyLIIVPLSTLSNWTYE-FDKWAPSVVKISYKGTPAMRRSLVPQLRSg 832
Cdd:cd18011   21 LLADEVGLGKTIEAGLIIKELLlrgDAKRV----LILCPASLVEQWQDElQDKFGLPFLILDRETAAQLRRLIGNPFEE- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  833 kFNVLLTTYEYI---IKDKHILAKIRWKYMIVDEGHRMKNHHC-------KLTQVLNTHyvAPRRILLTGTPLQNKLPEL 902
Cdd:cd18011   96 -FPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEEDF 172
                        170
                 ....*....|..
gi 51593084  903 WALLNFLLPTIF 914
Cdd:cd18011  173 RALLSLLDPGRF 184
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1398-1485 9.75e-19

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: 82.36  E-value: 9.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   1398 MNAIIDTVINykdssgRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLE 1477
Cdd:pfam00439    1 CLEILDKLME------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGP 74

                   ....*...
gi 51593084   1478 GSQIYEDS 1485
Cdd:pfam00439   75 GSVIYKAA 82
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1398-1492 8.45e-17

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: 77.28  E-value: 8.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1398 MNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLE 1477
Cdd:cd05522    6 IKNILKGLRKERDENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNEN 85
                         90
                 ....*....|....*
gi 51593084 1478 GSQIYEDSIVLQSVF 1492
Cdd:cd05522   86 DSQEYKDAVLLEKEA 100
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1393-1490 1.26e-16

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: 76.98  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1393 KLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNhkYRSLGDLEKDVMLLCHNAQ 1472
Cdd:cd05521    1 KLSKKLKPLYDGIYTLKEENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNAR 78
                         90
                 ....*....|....*...
gi 51593084 1473 TFNLEGSQIYEDSIVLQS 1490
Cdd:cd05521   79 LYNTKGSVIYKYALILEK 96
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1373-1494 3.03e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 82.55  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1373 EKAKKRRGRPPAEKLspnppKLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNH 1452
Cdd:COG5076  127 KTSVKKRKTPKIEDE-----LLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNG 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 51593084 1453 KYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1494
Cdd:COG5076  202 RYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLK 243
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
600-643 3.09e-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: 3.09e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 51593084    600 QMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 643
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
735-909 4.42e-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: 4.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVslynnNLNGILADEMGLGKTIQTIALItylMEHKRLNGPY--------------------------- 787
Cdd:cd18070    1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALI---LLHPRPDNDLdaadddsdemvccpdclvaetpvsska 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  788 -LIIVPLSTLSNWTYEFDKWAPSVVKIS-YKG---TPAMRRSLVPQLRSgkFNVLLTTYEYIIKDKHI------------ 850
Cdd:cd18070   73 tLIVCPSAILAQWLDEINRHVPSSLKVLtYQGvkkDGALASPAPEILAE--YDIVVTTYDVLRTELHYaeanrsnrrrrr 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51593084  851 ----------LAKIRWKYMIVDEghrMKNHHCKLTQVLNTHYVAPR--RILLTGTPLQNKLPELWALLNFL 909
Cdd:cd18070  151 qkryeappspLVLVEWWRVCLDE---AQMVESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFL 218
BRK smart00592
domain in transcription and CHROMO domain helicases;
601-643 1.73e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 1.73e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51593084     601 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 643
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPR 43
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1393-1499 2.67e-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: 67.19  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1393 KLTKQMNAIIDTVINYKDSSGrqlsevFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQ 1472
Cdd:cd05509    1 PLYTQLKKVLDSLKNHKSAWP------FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCR 74
                         90       100
                 ....*....|....*....|....*..
gi 51593084 1473 TFNLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:cd05509   75 LYNGPDTEYYKCANKLEKFFWKKLKEL 101
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1393-1497 3.36e-13

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: 67.41  E-value: 3.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1393 KLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQ 1472
Cdd:cd05525    2 RLAQVLKEICDAIITYKDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAE 81
                         90       100
                 ....*....|....*....|....*
gi 51593084 1473 TFNLEGSQIYEDSIVLQSVFKSARQ 1497
Cdd:cd05525   82 KYYGRKSPIGRDVCRLRKAYYQAKH 106
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
735-925 8.51e-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: 69.30  E-value: 8.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSlynNNLNGILADeMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSN-WTYEFDKW-APSVVK 812
Cdd:cd18013    1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWnHLRNLT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  813 ISYK-GTPAMRRSLVpqlrSGKFNVLLTTYEyIIKDKHILAKIRWKY--MIVDEGHRMKNHHCKLTQVLNTH-YVAPRRI 888
Cdd:cd18013   76 VSVAvGTERQRSKAA----NTPADLYVINRE-NLKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 51593084  889 LLTGTPLQNKLPELWALLNFL--LPTIFKSCSTF-EQWFN 925
Cdd:cd18013  151 GLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1420-1501 1.17e-12

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: 65.88  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1420 FIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1499
Cdd:cd05504   33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQRFFIKRCRKL 112

                 ..
gi 51593084 1500 AK 1501
Cdd:cd05504  113 GL 114
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-207 2.13e-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: 62.74  E-value: 2.13e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 51593084    173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1424-1494 2.65e-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: 61.53  E-value: 2.65e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51593084 1424 PSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1494
Cdd:cd05499   30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFND 100
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
172-206 8.60e-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: 55.23  E-value: 8.60e-10
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 51593084     172 SPFSPVQLHQLRAQILAYK-MLARGQPLPETLQLAV 206
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1428-1475 1.43e-09

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: 56.98  E-value: 1.43e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 51593084 1428 DLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1475
Cdd:cd05528   32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1430-1481 2.10e-09

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: 56.96  E-value: 2.10e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51593084 1430 PEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQI 1481
Cdd:cd05529   59 PDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEI 110
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1427-1494 5.46e-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: 55.07  E-value: 5.46e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51593084 1427 KDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1494
Cdd:cd05503   28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1414-1499 2.13e-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: 53.45  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1414 RQLSEVFIQLPSR-------KDLPEYYELIRKPVDFKKIKERIR----NHkYRSLGDLEKDVMLLCHNAQTFNLEGSQIY 1482
Cdd:cd05502   11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpkspQH-YSSPEEFVADVRLMFKNCYKFNEEDSEVA 89
                         90
                 ....*....|....*..
gi 51593084 1483 EDSIVLQSVFKSARQKI 1499
Cdd:cd05502   90 QAGKELELFFEEQLKEI 106
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1430-1475 2.29e-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: 2.29e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 51593084 1430 PEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1475
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 ...
1424-1493 3.73e-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: 52.67  E-value: 3.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1424 PSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFK 1493
Cdd:cd05498   30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1427-1500 4.03e-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: 53.04  E-value: 4.03e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51593084 1427 KDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIyedSIVLQSVFKSARQKIA 1500
Cdd:cd05511   28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVY---TKKAKEMLELAEELLA 98
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
1401-1501 8.16e-08

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: 51.98  E-value: 8.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1401 IIDTVINYKDSSGRQLSEVFIQLPSRKDLPEyyELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQ 1480
Cdd:cd05526   11 LFVSVMNHQDEEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSE 88
                         90       100
                 ....*....|....*....|.
gi 51593084 1481 IYEDSIVLQSVFKSARQKIAK 1501
Cdd:cd05526   89 IYEDAVELQQFFIKIRDELCK 109
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1395-1500 2.36e-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: 50.50  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1395 TKQMNAIIDTVInyKDSSGRQLSEVFiQLP---SRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNA 1471
Cdd:cd05497    3 TNQLQYLLKVVL--KALWKHKFAWPF-QQPvdaVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNC 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 51593084 1472 QTFNLEGsqiyeDSIVL--QSVFKSARQKIA 1500
Cdd:cd05497   80 YIYNKPG-----DDVVLmaQTLEKLFLQKLA 105
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
755-893 2.45e-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: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  755 NGILADEMGLGKTIQTIALITYLMEHKRlnGPYLIIVPLSTLSNWTYE-FDKWAPSVVKISYKgTPAMRRSLVPQLRSGK 833
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAErLRELFGPGIRVAVL-VGGSSAEEREKNKLGD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51593084  834 FNVLLTTYEYIIKDKHILAKI---RWKYMIVDEGHRM----KNHHCKLTQVLNTHYVAPRRILLTGT 893
Cdd:cd00046   80 ADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
PHA03378 PHA03378
EBNA-3B; Provisional
74-393 3.67e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.07  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    74 HKPMDG-------IHDKGIVEDVHCGSMKGTSMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPISGGGPTPP 146
Cdd:PHA03378  530 PQPRAGrrapcvyTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWPV 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   147 QMPPSQPG-----ALIPgdpqAMNQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGMQQQQ 219
Cdd:PHA03378  600 PHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPYQ 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   220 QQQQQQQQQQQQQQQQQQQQQQPQQPQQQAQAQPQQQQQQQQQPALVSYNRPSG-PGQELLLSGQSAPQKLSAPAPSGRP 298
Cdd:PHA03378  676 PSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAaPGRARPPAAAPGRARPPAAAPGRAR 755
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   299 SPAPQAAVQPTATAVPG-PSVQQPAPGQPSPvlqLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELESL 375
Cdd:PHA03378  756 PPAAAPGRARPPAAAPGaPTPQPPPQAPPAP---QQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGG 832
                         330
                  ....*....|....*...
gi 51593084   376 PGSLPPDLRTKATVELKA 393
Cdd:PHA03378  833 VKRGRPSLKKPAALERQA 850
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1424-1494 5.20e-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: 49.25  E-value: 5.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51593084 1424 PSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1494
Cdd:cd05506   27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIFET 97
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1424-1492 7.34e-07

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: 49.23  E-value: 7.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51593084 1424 PSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVF 1492
Cdd:cd05500   31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
ResIII pfam04851
Type III restriction enzyme, res subunit;
734-894 7.49e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 50.75  E-value: 7.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    734 TLKHYQLQGLE-WMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVP-LSTLSNWTYEFDKWAPSVV 811
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    812 KIS--YKGtpamrRSLVPQLRSGKfnVLLTTYEYIIKD----KHILAKIRWKYMIVDEGHRM--KNHhcklTQVLNtHYV 883
Cdd:pfam04851   82 EIGeiISG-----DKKDESVDDNK--IVVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE-YFK 149
                          170
                   ....*....|.
gi 51593084    884 APRRILLTGTP 894
Cdd:pfam04851  150 PAFLLGLTATP 160
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1418-1475 8.01e-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: 48.93  E-value: 8.01e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 51593084 1418 EVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1475
Cdd:cd05512   20 EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYN 77
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1417-1501 1.62e-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: 48.61  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1417 SEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNL-EGSQIYEDSIVLQSVFKSA 1495
Cdd:cd05496   23 SEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTPnKRSRIYSMTLRLSALFEEH 102

                 ....*.
gi 51593084 1496 RQKIAK 1501
Cdd:cd05496  103 IKKIIS 108
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1424-1494 2.09e-06

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: 47.82  E-value: 2.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51593084 1424 PSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1494
Cdd:cd05495   31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQ 101
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
735-894 4.00e-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: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  735 LKHYQLQGLEWMVSLYNNNLnGILADEMGLGKTIQTIALITYLMEHKrlngpYLIIVP-LSTLSNWTYEFDKWAPSVVki 813
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRR-GILVLPTGSGKTLTALALIAYLKELR-----TLIVVPtDALLDQWKERFEDFLGDSS-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  814 sykgtpamrrslVPQLRSGK------FNVLLTTYEYIIKDKHILAKI--RWKYMIVDEGHrmknHHC--KLTQVLnTHYV 883
Cdd:cd17926   73 ------------IGLIGGGKkkdfddANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KELN 135
                        170
                 ....*....|.
gi 51593084  884 APRRILLTGTP 894
Cdd:cd17926  136 AKYRLGLTATP 146
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1344-1439 6.99e-06

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: 46.67  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1344 NLEEMEEEVRLKKRKRRrNVDKDPVKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDTVInyKDSSGRQlsevfIQL 1423
Cdd:cd05494    1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETGA--RDLEDLQ-----IVQ 70
                         90
                 ....*....|....*.
gi 51593084 1424 PSRKDLPEYYELIRKP 1439
Cdd:cd05494   71 EDPADKQIDDEGRRSP 86
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1402-1475 9.48e-06

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: 46.28  E-value: 9.48e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51593084 1402 IDTVINYKDSSGRQlSEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1475
Cdd:cd05510   12 LDKVLNELKTYTEH-STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1417-1475 1.02e-05

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: 45.82  E-value: 1.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 51593084 1417 SEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1475
Cdd:cd05507   21 ASVFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
732-894 1.80e-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: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  732 NGTLKHYQLQGLE-WMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLngpyLIIVPLSTLSN-WTYEFDKWAPS 809
Cdd:COG1061   78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  810 VVKISYKgtpamrrslvpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVA 884
Cdd:COG1061  154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPA 213
                        170
                 ....*....|
gi 51593084  885 PRRILLTGTP 894
Cdd:COG1061  214 AYRLGLTATP 223
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
22-461 2.36e-05

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: 49.38  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     22 SPGPILGPSPGPGPSPGSVHSMMGPSP-----GPPSVSHPLSTMGSADFPQEGMHQLHKPmdgihdKGIVEDVHCGSMKG 96
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQPSLHGQMPPMPhslqtGPSHMQHPVPPQPFPLTPQSSQSQVPPG------PSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     97 TSmrPPHPGMGPPQSPMDQ------HSQGYMSPHP----SPLGAPEHVSSPISGGGPTPPQMPPS--QPGALIPGDPQAM 164
Cdd:pfam03154  327 TP--PSQSQLQSQQPPREQplppapLSMPHIKPPPttpiPQLPNPQSHKHPPHLSGPSPFQMNSNlpPPPALKPLSSLST 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    165 NQPNRGPSPfsPVQLhqlraqilaykmLARGQPLPETlqlAVQGkrtlPGMQQQQQqqqqqqqqqqqqqqqqqqqqqpqq 244
Cdd:pfam03154  405 HHPPSAHPP--PLQL------------MPQSQQLPPP---PAQP----PVLTQSQS------------------------ 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    245 pqqqaqaqpqqqqqqqqqpalVSYNRPSGPGQELLLSGQSAPQKLSAPAPSGRPSPAPQAAVQPTATAVPGPSVQQPAPG 324
Cdd:pfam03154  440 ---------------------LPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    325 QPSPVLQLQQKQSRISPiqkpqgldPVEILQEreyrlqariahRIQELESlPGSLPPDLR------TKATVELKALRLLN 398
Cdd:pfam03154  499 SVSSSGPVPAAVSCPLP--------PVQIKEE-----------ALDEAEE-PESPPPPPRspspepTVVNTPSHASQSAR 558
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51593084    399 FQRQLRQEVVACMRRDTTLETALNSK-------AYKRSKRQTLREARMTEKLEKQQKIEQERKR-RQKHQE 461
Cdd:pfam03154  559 FYKHLDRGYNSCARTDLYFMPLAGSKlakkreeALEKAKREAEQKAREEKEREKEKEKEREREReREREAE 629
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
44-327 3.11e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.85  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     44 MGPSPGPPS---------VSHPLSTMGSADFPQEGMHQLHkPMDGIhdkgivedvhcgsmkgTSMRPPHpGMGPPQSPMD 114
Cdd:pfam09606  102 MGPGPGGPMgqqmggpgtASNLLASLGRPQMPMGGAGFPS-QMSRV----------------GRMQPGG-QAGGMMQPSS 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    115 QHSQGYMSPHPSPLGAPEH--VSSPISGGGPTPPQMPPSQ---PGALIPGDPQA-MNQPNRGPSPFSPVQLHQLRAQILA 188
Cdd:pfam09606  164 GQPGSGTPNQMGPNGGPGQgqAGGMNGGQQGPMGGQMPPQmgvPGMPGPADAGAqMGQQAQANGGMNPQQMGGAPNQVAM 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    189 YKMLARGQPLPETLQLAV---------------QGKRTLPGMQQQQQQQQQQQQQQQQQQQQQQQQQQPQQPQQQAQAQP 253
Cdd:pfam09606  244 QQQQPQQQGQQSQLGMGInqmqqmpqgvgggagQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHP 323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    254 QQQQQQQQQPALVSYNRPSGPGQELLLSGQSA--------PQKLSAPAPSGRPSPAPQAAVQPTAT---AVPGPSVQQPA 322
Cdd:pfam09606  324 AAHQQQMNQSVGQGGQVVALGGLNHLETWNPGnfgglganPMQRGQPGMMSSPSPVPGQQVRQVTPnqfMRQSPQPSVPS 403

                   ....*
gi 51593084    323 PGQPS 327
Cdd:pfam09606  404 PQGPG 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
351-562 3.76e-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: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  351 VEILQEREYRLQARIAHRIQELESLPGSLpPDLRTKATVELKALRLLNFQRQLRQEVVAcmRRDTTLETALNSKAYKRSK 430
Cdd:COG1196  283 LEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAE 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  431 RQTLREARMTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIE 510
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51593084  511 KERMRRLMAEDEEGYRKLIDQKKDRRLAyLLQQTDEYVANLTNLVWEHKQAQ 562
Cdd:COG1196  440 EEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAA 490
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1128-1176 4.39e-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: 4.39e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 51593084 1128 SQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQ 1176
Cdd:cd18785   20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
763-894 5.58e-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: 5.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    763 GLGKTIqtIALITYL-MEHKRLNGPY-LIIVPLSTLSNWTYE-FDKWAPSV---VKISYKGTPamRRSLVPQLRSGkfNV 836
Cdd:pfam00270   24 GSGKTL--AFLLPALeALDKLDNGPQaLVLAPTRELAEQIYEeLKKLGKGLglkVASLLGGDS--RKEQLEKLKGP--DI 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084    837 LLTTYE---YIIKDKHILAKIrwKYMIVDEGHRM--KNHHCKLTQVLNTHYVAPRRILLTGTP 894
Cdd:pfam00270   98 LVGTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
Bromo_ZMYND11 cd05492
Bromodomain; ZMYND11_like sub-family. ZMYND11 or BS69 is a ubiquitously expressed nuclear ...
1428-1483 6.13e-05

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: 43.91  E-value: 6.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 51593084 1428 DLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYE 1483
Cdd:cd05492   35 KLPKRRRLIHTHLDVADIQEKINSEKYTSLEEFKADALLLLHNTAIFHGADSEQYD 90
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1401-1481 1.05e-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: 42.91  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1401 IIDTVINYKDSsgrqlsEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQ 1480
Cdd:cd05505    8 ILSKILKYRFS------WPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYYENGSY 81

                 .
gi 51593084 1481 I 1481
Cdd:cd05505   82 V 82
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
46-347 1.68e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 46.15  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     46 PSPGPPSVSHPLSTMGSADFPQEGMHQLHKPMDGIHDKGIVEDVHCGSMKGTSMrpphPGMGPPQSPMDQHSQGYMSPHP 125
Cdd:pfam09606  156 GGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGM----PGPADAGAQMGQQAQANGGMNP 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    126 SPL-GAPEHVsspISGGGPTPPQMPPSQPGALiPGDPQAMNQPNRGPS----PFSPVQLHQLRAQILAYKMLARGQPLPE 200
Cdd:pfam09606  232 QQMgGAPNQV---AMQQQQPQQQGQQSQLGMG-INQMQQMPQGVGGGAgqggPGQPMGPPGQQPGAMPNVMSIGDQNNYQ 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    201 TLQLAVQGKRtlpgmqqqqqqQQQQQQQQQQQQQQQQQQQQPQQPQQQAQAQPQQQQQQQQQPALVSynrPSGPGQELLL 280
Cdd:pfam09606  308 QQQTRQQQQQ-----------QGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAN---PMQRGQPGMM 373
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51593084    281 SGQS---APQKLSAPAPSG-RPSPAPQAAVQPTATAVPGPSV---QQPAPG---QPSPVLQLQQKQSRISPIQKPQG 347
Cdd:pfam09606  374 SSPSpvpGQQVRQVTPNQFmRQSPQPSVPSPQGPGSQPPQSHpggMIPSPAlipSPSPQMSQQPAQQRTIGQDSPGG 450
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
100-176 2.93e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 43.10  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    100 RPPHPGMGPPQSPMDQHsqgymsPHPSPLGAPEHvsSPISGG-----GPTPPQMPPSQPGALIPGDPQAMNQPNRGPSPF 174
Cdd:pfam15240   48 GPPPGGFPPQPPASDDP------PGPPPPGGPQQ--PPPQGGkqkpqGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPG 119

                   ..
gi 51593084    175 SP 176
Cdd:pfam15240  120 KP 121
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
99-203 3.51e-04

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: 45.53  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     99 MRPPHPGMGPPQSPMDQHSQ-GYMSPHPSPLGAPEHVSSPISggGPTPPQMPPSQPGALIPGDPQAmnQPNRGPSPFSPV 177
Cdd:pfam03154  174 LQAQSGAASPPSPPPPGTTQaATAGPTPSAPSVPPQGSPATS--QPPNQTQSTAAPHTLIQQTPTL--HPQRLPSPHPPL 249
                           90       100       110
                   ....*....|....*....|....*....|....
gi 51593084    178 QL-------HQLRAQILAYKML-ARGQPLPETLQ 203
Cdd:pfam03154  250 QPmtqppppSQVSPQPLPQPSLhGQMPPMPHSLQ 283
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
763-862 4.02e-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: 43.08  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084  763 GLGKTiqTIALITYLMEHKRlNGPYLIIVPLSTLSNWTYE----FDKWAPSVVKI--SYKGTPAMRR-SLVPQLRSGKFN 835
Cdd:cd17924   42 GVGKT--TFGLATSLYLASK-GKRSYLIFPTKSLVKQAYErlskYAEKAGVEVKIlvYHSRLKKKEKeELLEKIEKGDFD 118
                         90       100
                 ....*....|....*....|....*..
gi 51593084  836 VLLTTYEYIIKDKHILAKIRWKYMIVD 862
Cdd:cd17924  119 ILVTTNQFLSKNFDLLSNKKFDFVFVD 145
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
41-165 4.51e-04

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: 44.42  E-value: 4.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     41 HSMMgPSPgppsvshPLSTMGSADFPQegmhQLHKPMdgiHDKGIvedvhcgsmkGTSMRPPHPGmGPPQSPMDQHSQG- 119
Cdd:pfam15279  192 PSSM-PPP-------FLRPPPSIPQPN----SPLSNP---MLPGI----------GPPPKPPRNL-GPPSNPMHRPPFSp 245
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 51593084    120 --YMSPHPSPLGAPEhvSSPISGGGPTPPQMPPSQPGALIPgDPQAMN 165
Cdd:pfam15279  246 hhPPPPPTPPGPPPG--LPPPPPRGFTPPFGPPFPPVNMMP-NPPEMN 290
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
344-536 5.18e-04

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: 45.06  E-value: 5.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    344 KPQGLDPVEILQEREY-------RLQARIAHRIQELESLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTT 416
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    417 LETALnskAYKRSKRQTLRE--ARMTEKLEKQQKIEQERKRRQKHQEyLNSILQHAKDFKEYHRSVAGKIQKLskavatw 494
Cdd:TIGR02169  749 LEQEI---ENVKSELKELEAriEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSKLEEEVSRIEARLREI------- 817
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 51593084    495 hanterEQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRR 536
Cdd:TIGR02169  818 ------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
315-546 1.17e-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: 43.40  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    315 GPSVQQPapgQPSPVLQLQQKQ----SRISPIQKPQGLDPVEILQEREYRL--QARIAHRIQELESlpgslppdlRTKAT 388
Cdd:pfam15709  272 DSVVEDP---WLSSKYDAEESQvsidGRSSPTQTFVVTGNMESEEERSEEDpsKALLEKREQEKAS---------RDRLR 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    389 VELKALRLLNF---------QRQLRQEVvacMRRDTTLETALNSKAYKRSKRQTLREARMTEklEKQQKIEQERKRRQKH 459
Cdd:pfam15709  340 AERAEMRRLEVerkrreqeeQRRLQQEQ---LERAEKMREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQL 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    460 QEYLNSILQHAKdfkEYHRSVAgKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMAEDEEgyrklidqkkdRRLAY 539
Cdd:pfam15709  415 QAAQERARQQQE---EFRRKLQ-ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-----------ERLEY 479

                   ....*..
gi 51593084    540 LLQQTDE 546
Cdd:pfam15709  480 QRQKQEA 486
PTZ00121 PTZ00121
MAEBL; Provisional
424-535 1.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   424 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHAntEREQK 503
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                          90       100       110
                  ....*....|....*....|....*....|..
gi 51593084   504 KETERIEKERMRRlmaedEEGYRKLIDQKKDR 535
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
Herpes_TAF50 pfam03326
Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 ...
271-409 2.94e-03

Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 and similar ORF 50 proteins from other herpesviruses.


Pssm-ID: 308764 [Multi-domain]  Cd Length: 568  Bit Score: 41.99  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    271 PSGPGQELLLSGQSAPQKLSA---PAPSGRPSPAPQaAVQPTATAVP-GPSVQQPaPGQPSPvlQLQQKQSRISPIQKPQ 346
Cdd:pfam03326  430 PGSPSANRPLPSSLAPTPTGPvhePGSSLTPATVPQ-PLDAAPVATPeASHELQP-PDEETP--QPLDEDQALCGQQDAS 505
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084    347 GLDPVEILQEREYRLQARiahriQELESLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVA 409
Cdd:pfam03326  506 HPPPRGQLDELTTTLESM-----TEDLNLDSPLSPEDNEILETILNDLYPEERRQQEQQHSQG 563
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
45-173 3.88e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.02  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084     45 GPSPGPPSVSHPLSTMGSADFPQEGMHQlhKPMDGIHDKGivedvHCGSMKGTSMRPPHPGMGPPQSPMDQhsQGYMSPH 124
Cdd:pfam15240   48 GPPPGGFPPQPPASDDPPGPPPPGGPQQ--PPPQGGKQKP-----QGPPPQGGPRPPPGKPQGPPPQGGNQ--QQGPPPP 118
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 51593084    125 PSPLGAPEHVSSPISGGGPT--PPQMPPSQPgaliPGDPQAMNQPNRGPSP 173
Cdd:pfam15240  119 GKPQGPPPQGGGPPPQGGNQqgPPPPPPGNP----QGPPQRPPQPGNPQGP 165
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1417-1499 4.07e-03

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: 38.13  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084 1417 SEVFIQLPSRKDLPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSivlQSVFKSAR 1496
Cdd:cd05508   20 AEPFLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYNGGDHKLTQAA---KAIVKICE 96

                 ...
gi 51593084 1497 QKI 1499
Cdd:cd05508   97 QEM 99
PHA03378 PHA03378
EBNA-3B; Provisional
47-356 4.78e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084    47 SPGPPSV-SHPLSTmgsADFPQEGMHQLHKPMDGIHDKGIVEDVHCGSmkgTSMRPPHPGMGPPQSPMDQhsQGYMSPHP 125
Cdd:PHA03378  605 TPEPPTTqSHIPET---SAPRQWPMPLRPIPMRPLRMQPITFNVLVFP---TPHQPPQVEITPYKPTWTQ--IGHIPYQP 676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   126 SPLGApeHVSSPISGGgPTPPQMPPSQPGALIP--GDPQAMNQPNRGPSPFSPVQLHQLRAQILAykmlarGQPLPETLQ 203
Cdd:PHA03378  677 SPTGA--NTMLPIQWA-PGTMQPPPRAPTPMRPpaAPPGRAQRPAAATGRARPPAAAPGRARPPA------AAPGRARPP 747
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   204 LAVQGKRTLPgmqQQQQQQQQQQQQQQQQQQQQQQQQQPQQPQQQAQAQPQQQQQQQQQPALVSYNRPSGPGQElLLSGQ 283
Cdd:PHA03378  748 AAAPGRARPP---AAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQ-GPTKQ 823
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51593084   284 SAPQKLSAPAPSGRPSPAPQAAVQPTATAVPGPSvqqPAPGQPSPVLQlqqkqsriSPIQKPQGLDPVEILQE 356
Cdd:PHA03378  824 ILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPS---PGSGTSDKIVQ--------APVFYPPVLQPIQVMRQ 885
PHA03247 PHA03247
large tegument protein UL36; Provisional
100-357 7.65e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   100 RPPHPGMGP-----------PQSPMDQHSQGYMSPHPSPLGAPEHVSSPISGGGPTPPQMPPSQPGALIPGDPQAmnqPN 168
Cdd:PHA03247 2700 DPPPPPPTPepaphalvsatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA---PA 2776
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   169 RGPSPFSPVQLHQLRAQILAYKMLARG---QPLPETLQLAVQGKRTLPGMQQQQQQQQQQQQQQQQQQQQQQQQQQP--- 242
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsv 2856
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   243 ------QQPQQQAQAQPQQQQQQQQQPALVSYNRPSGPGQELLLSgQSAPQKLSAPAPSGRPSPAPQAAVQPTATAVPGP 316
Cdd:PHA03247 2857 apggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALP-PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 51593084   317 SVQQPAPGQPSPVLQLQQKQSRISPIQKPQGLDPVEILQER 357
Cdd:PHA03247 2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR 2976
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
282-372 9.25e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 40.28  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51593084   282 GQSAPQKLSAPAPSGRPSPAPQAAVQPTATAVPGPSVQQPAPGQPSPVLQLQQKQSRISPIQKPQG--LDPVEILQE-RE 358
Cdd:PRK01297   12 GEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASLWKLEDfvVEPQEGKTRfHD 91
                          90
                  ....*....|....
gi 51593084   359 YRLQARIAHRIQEL 372
Cdd:PRK01297   92 FNLAPELMHAIHDL 105
 
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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