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Conserved domains on  [gi|1207168553|ref|XP_021325403|]
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SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4a isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
743-993 2.36e-169

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: 510.36  E-value: 2.36e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  743 YYAVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIV 822
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  823 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHH 902
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  903 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 982
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1207168553  983 VLRPFLLRRLK 993
Cdd:cd18062    241 VLRPFLLRRLK 251
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
762-1244 7.42e-160

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: 513.58  E-value: 7.42e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  762 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSV 841
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  842 VKVSYKGSPAARRAFLP-ILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 917
Cdd:PLN03142   246 RAVKFHGNPEERAHQREeLLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  918 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 997
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  998 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEESfsehlg 1076
Cdd:PLN03142   392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1077 ftGGIVQGSDLYRASGKFELLDRILPKLRATNHKVLLFCQMTTLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFND 1156
Cdd:PLN03142   458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1157 PSHQYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1236
Cdd:PLN03142   536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                   ....*...
gi 1207168553 1237 DQKVIQAG 1244
Cdd:PLN03142   616 DALVIQQG 623
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1440-1545 4.54e-61

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: 203.81  E-value: 4.54e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQT 81
                           90       100
                   ....*....|....*....|....*.
gi 1207168553 1520 FNLEGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:cd05516     82 FNLEGSLIYEDSIVLQSVFKSARQKI 107
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1301-1368 1.37e-23

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: 95.40  E-value: 1.37e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1301 DRRREEARNPK-RRPRLMEEDELPTWIMKDDAEVERLTCEEEEEKMFGRGSRQRKEVDYSDSLTEKQWL 1368
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
478-550 2.10e-23

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.16  E-value: 2.10e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553   478 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 550
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
629-672 1.44e-15

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: 71.77  E-value: 1.44e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1207168553  629 QMSDLPVKVIHVDSGKILTGMDAPKAGQLDTWLEMNPGYEVAPR 672
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 ...
198-231 5.64e-13

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: 64.28  E-value: 5.64e-13
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207168553  198 FNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 231
Cdd:pfam08880    2 FTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
382-624 1.63e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  382 VEILQEREY-------RLQARIAHRIQELENLPGSLAgdlRTKANIELKALRLLNFQRQLRQEvvvcmrrDTALETALNA 454
Cdd:COG1196    283 LEEAQAEEYellaelaRLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEEL-------EEELEEAEEE 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  455 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQK 534
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  535 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQALKDKKKKKKKKKPENAEGGA 614
Cdd:COG1196    433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
                          250
                   ....*....|
gi 1207168553  615 PALGPDGEPL 624
Cdd:COG1196    512 AALLLAGLRG 521
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
65-360 1.47e-06

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 53.09  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   65 PQDNMHQMHKPMEGMHEKGIPEDQRYGQMKGMGMRQGGHSGMGPPPS---PMDQHSQGYPSPLGGSDHAPSPVPANGPPS 141
Cdd:pfam09606  151 PGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGgqmPPQMGVPGMPGPADAGAQMGQQAQANGGMN 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  142 GPMMPSGPGAMPMEGGDPQAMAQQNR--------------SGGAGGVAGPGpsggppnaggpggaggptpfNQNQLHQLR 207
Cdd:pfam09606  231 PQQMGGAPNQVAMQQQQPQQQGQQSQlgmginqmqqmpqgVGGGAGQGGPG--------------------QPMGPPGQQ 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  208 AQIMAYKMLARGQPLPDHLQMAVQGKR---PMPGMQQGMPNMP--PASGQGAGPPGPGVPGPGGPNY----------NRP 272
Cdd:pfam09606  291 PGAMPNVMSIGDQNNYQQQQTRQQQQQqggNHPAAHQQQMNQSvgQGGQVVALGGLNHLETWNPGNFgglganpmqrGQP 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  273 HGMVGPNMPPPGPSGVPPGLQGQPTNGPPK-PWPEGPMVNaaAPASAPQKLIPPqPTGRPSPAPPSVPPAASPVMPPQtQ 351
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQPSvPSPQGPGSQ--PPQSHPGGMIPS-PALIPSPSPQMSQQPAQQRTIGQ-D 446

                   ....*....
gi 1207168553  352 SPGQPAQPP 360
Cdd:pfam09606  447 SPGGSLNTP 455
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
743-993 2.36e-169

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: 510.36  E-value: 2.36e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  743 YYAVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIV 822
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  823 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHH 902
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  903 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 982
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1207168553  983 VLRPFLLRRLK 993
Cdd:cd18062    241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
762-1244 7.42e-160

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 513.58  E-value: 7.42e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  762 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSV 841
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  842 VKVSYKGSPAARRAFLP-ILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 917
Cdd:PLN03142   246 RAVKFHGNPEERAHQREeLLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  918 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 997
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  998 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEESfsehlg 1076
Cdd:PLN03142   392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1077 ftGGIVQGSDLYRASGKFELLDRILPKLRATNHKVLLFCQMTTLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFND 1156
Cdd:PLN03142   458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1157 PSHQYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1236
Cdd:PLN03142   536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                   ....*...
gi 1207168553 1237 DQKVIQAG 1244
Cdd:PLN03142   616 DALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
546-1228 4.77e-122

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 399.21  E-value: 4.77e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  546 RRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRAHKAAQALKDKKKKKKKKKPENAEGGAPALGPDGEPLD 625
Cdd:COG0553     24 LRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  626 ETSQMSDLPVKVIHVDSGKILTGMDAPKAGQLDTWLEMNPGYEVAPRSDSEDSGSDEEEDDEEEPQPSQAPTEEKKVIPD 705
Cdd:COG0553    104 LALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  706 PDSEDVSEVDARHIIEHAKQDVDDEYGNSAFIRGLQSYYAVAHAVTEKVEKQSSLlvNGQLKQYQIKGLEWLVSLYNNNL 785
Cdd:COG0553    184 LALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  786 NGILADEMGLGKTIQTIALITYLMEfKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFLPIlrsGKF 865
Cdd:COG0553    262 GGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPF---EDA 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  866 NVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNThyL-APRRVLLTGTPLQNKLPELWALLNFLLPTI 944
Cdd:COG0553    338 DLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA--LkARHRLALTGTPVENRLEELWSLLDFLNPGL 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  945 FKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMq 1024
Cdd:COG0553    416 LGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV- 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1025 akgVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHlgftggivqgsdlyraSGKFELLDRILPKL 1104
Cdd:COG0553    485 ---LEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR----------------SAKLEALLELLEEL 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1105 RATNHKVLLFCQMTTLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFNDPShQYFIFLLSTRAGGLGLNLQSADTVI 1184
Cdd:COG0553    546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGP-EAPVFLISLKAGGEGLNLTAADHVI 624
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1207168553 1185 IFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1228
Cdd:COG0553    625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
769-1064 1.89e-112

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: 357.76  E-value: 1.89e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  769 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEFKRL-NGPFLIIVPLSTLSNWVYEFDKWA--PSVVKV 844
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  845 SYKGSPAARRAFLPIL-RSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRVLLTG 923
Cdd:pfam00176   81 VLHGNKRPQERWKNDPnFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  924 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 1003
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207168553 1004 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1064
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1440-1545 4.54e-61

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: 203.81  E-value: 4.54e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQT 81
                           90       100
                   ....*....|....*....|....*.
gi 1207168553 1520 FNLEGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:cd05516     82 FNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1091-1217 3.10e-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: 191.15  E-value: 3.10e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1091 SGKFELLDRILPKLRATNHKVLLFCQMTTLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFNDPShQYFIFLLSTRA 1170
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1207168553 1171 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1217
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
765-954 3.43e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.22  E-value: 3.43e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   765 QLKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEFKrlNGPFLIIVPLSTL-SNWVYEFDKWAPS-V 841
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   842 VKVSYKGSPAARRAFLPILRSGKFNVLVTTYEYIIKD--KQVLAKLRWKYMIVDEGHRMKN--HHCKLTQVLNTHYLAPR 917
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1207168553   918 RVLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 954
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
BROMO smart00297
bromo domain;
1438-1545 1.02e-28

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 111.60  E-value: 1.02e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  1438 PSLTKKMKKTVDAVIKYKDGngRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNA 1517
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|....*...
gi 1207168553  1518 QTFNLEGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1092-1206 1.11e-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: 111.53  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1092 GKFELLDRILPKLRatNHKVLLFCQMTTlmTIMEDYFAYR-NFKYLRLDGTTKAEDRGMLLKNFNDPSHQyfiFLLSTRA 1170
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1207168553 1171 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1206
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1301-1368 1.37e-23

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: 95.40  E-value: 1.37e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1301 DRRREEARNPK-RRPRLMEEDELPTWIMKDDAEVERLTCEEEEEKMFGRGSRQRKEVDYSDSLTEKQWL 1368
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
478-550 2.10e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.16  E-value: 2.10e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553   478 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 550
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
HELICc smart00490
helicase superfamily c-terminal domain;
1123-1206 4.51e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 4.51e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  1123 IMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFNDPShqyFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1202
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK---IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1207168553  1203 HRIG 1206
Cdd:smart00490   79 GRAG 82
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
479-545 6.16e-21

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


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 88.01  E-value: 6.16e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168553  479 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQKKENERIEKERM 545
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1460-1531 2.25e-18

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: 81.21  E-value: 2.25e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207168553 1460 RQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDS 1531
Cdd:pfam00439   11 HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAA 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1428-1545 6.71e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.39  E-value: 6.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1428 PPAEKLSPNPPS---LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLN 1504
Cdd:COG5076    128 TSVKKRKTPKIEdelLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFE 207
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1207168553 1505 DLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:COG5076    208 EFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEI 248
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
629-672 1.44e-15

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: 71.77  E-value: 1.44e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1207168553  629 QMSDLPVKVIHVDSGKILTGMDAPKAGQLDTWLEMNPGYEVAPR 672
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
630-672 9.52e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 66.60  E-value: 9.52e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1207168553   630 MSDLPVKVIHVDSGKILTGMDAPKAGQLDTWLEMNPGYEVAPR 672
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 ...
198-231 5.64e-13

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: 64.28  E-value: 5.64e-13
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207168553  198 FNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 231
Cdd:pfam08880    2 FTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
198-230 3.20e-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: 56.39  E-value: 3.20e-10
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1207168553   198 FNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 230
Cdd:smart00951    3 FTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
382-624 1.63e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  382 VEILQEREY-------RLQARIAHRIQELENLPGSLAgdlRTKANIELKALRLLNFQRQLRQEvvvcmrrDTALETALNA 454
Cdd:COG1196    283 LEEAQAEEYellaelaRLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEEL-------EEELEEAEEE 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  455 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQK 534
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  535 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQALKDKKKKKKKKKPENAEGGA 614
Cdd:COG1196    433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
                          250
                   ....*....|
gi 1207168553  615 PALGPDGEPL 624
Cdd:COG1196    512 AALLLAGLRG 521
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
763-925 1.01e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 53.49  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  763 NGQLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLngpfLIIVPLSTLSN-WVYEFDKWAPS 840
Cdd:COG1061     78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  841 VVKVSYKgspaarraflpilRSGKFNVLVTTYEYIIKDKQvLAKL--RWKYMIVDEGhrmknHHC---KLTQVLNtHYLA 915
Cdd:COG1061    154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEA-----HHAgapSYRRILE-AFPA 213
                          170
                   ....*....|
gi 1207168553  916 PRRVLLTGTP 925
Cdd:COG1061    214 AYRLGLTATP 223
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
65-360 1.47e-06

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: 53.09  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   65 PQDNMHQMHKPMEGMHEKGIPEDQRYGQMKGMGMRQGGHSGMGPPPS---PMDQHSQGYPSPLGGSDHAPSPVPANGPPS 141
Cdd:pfam09606  151 PGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGgqmPPQMGVPGMPGPADAGAQMGQQAQANGGMN 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  142 GPMMPSGPGAMPMEGGDPQAMAQQNR--------------SGGAGGVAGPGpsggppnaggpggaggptpfNQNQLHQLR 207
Cdd:pfam09606  231 PQQMGGAPNQVAMQQQQPQQQGQQSQlgmginqmqqmpqgVGGGAGQGGPG--------------------QPMGPPGQQ 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  208 AQIMAYKMLARGQPLPDHLQMAVQGKR---PMPGMQQGMPNMP--PASGQGAGPPGPGVPGPGGPNY----------NRP 272
Cdd:pfam09606  291 PGAMPNVMSIGDQNNYQQQQTRQQQQQqggNHPAAHQQQMNQSvgQGGQVVALGGLNHLETWNPGNFgglganpmqrGQP 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  273 HGMVGPNMPPPGPSGVPPGLQGQPTNGPPK-PWPEGPMVNaaAPASAPQKLIPPqPTGRPSPAPPSVPPAASPVMPPQtQ 351
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQPSvPSPQGPGSQ--PPQSHPGGMIPS-PALIPSPSPQMSQQPAQQRTIGQ-D 446

                   ....*....
gi 1207168553  352 SPGQPAQPP 360
Cdd:pfam09606  447 SPGGSLNTP 455
PTZ00121 PTZ00121
MAEBL; Provisional
455-566 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  455 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHAntEREQK 534
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207168553  535 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 566
Cdd:PTZ00121  1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
383-568 4.52e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  383 EILQEREyRLQARIAHRIQELEnlpgslagdlRTKANIElkALRLlnfqrQLRQEVVVCMRRDTALETALNakayKRSKR 462
Cdd:pfam13868  177 EIEEEKE-REIARLRAQQEKAQ----------DEKAERD--ELRA-----KLYQEEQERKERQKEREEAEK----KARQR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  463 QSLREARiteKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANT--EREQKKENERI 540
Cdd:pfam13868  235 QELQQAR---EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieEREEQRAAERE 311
                          170       180
                   ....*....|....*....|....*...
gi 1207168553  541 EKERMRRLMAEDEEGYRKLIDQKKDKRL 568
Cdd:pfam13868  312 EELEEGERLREEEAERRERIEEERQKKL 339
PHA03247 PHA03247
large tegument protein UL36; Provisional
107-381 8.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 8.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  107 GPPPSPMDQHSQGYP--SPLGGSDHAPSPvPANGPPSGPmmPSGPGAMPMEGGDPQAMAQQNRSGGAGGVAGPGPSGGPP 184
Cdd:PHA03247  2590 DAPPQSARPRAPVDDrgDPRGPAPPSPLP-PDTHAPDPP--PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  185 NAGGPGGAGGPTPFNQNQLHQLRAQIMAYKMLARGQPlpdhlqmavQGKRPMPGMQQGMPNMPPASGQGAGPPGPGVPGP 264
Cdd:PHA03247  2667 ARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP---------PPPTPEPAPHALVSATPLPPGPAAARQASPALPA 2737
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  265 GGPNYNRPHGMVGPNMPPPGPSGvppglqgQPTNGPPKPWPegpmvnAAAPASAPQKLIPPQPTGRPSPAPpsvppaasp 344
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARP-------PTTAGPPAPAP------PAAPAAGPPRRLTRPAVASLSESR--------- 2795
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1207168553  345 vmpPQTQSPGQPAQPPMVLHQKQNRITPIQKPRGLDP 381
Cdd:PHA03247  2796 ---ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
743-993 2.36e-169

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: 510.36  E-value: 2.36e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  743 YYAVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIV 822
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  823 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHH 902
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  903 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 982
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1207168553  983 VLRPFLLRRLK 993
Cdd:cd18062    241 VLRPFLLRRLK 251
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
763-993 9.84e-166

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: 499.59  E-value: 9.84e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  763 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVV 842
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  843 KVSYKGSPAARRAFLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNTHYLAPRRVLLT 922
Cdd:cd17996     81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553  923 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKV--DLNEEETILIIRRLHKVLRPFLLRRLK 993
Cdd:cd17996    161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
762-1244 7.42e-160

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 513.58  E-value: 7.42e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  762 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSV 841
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  842 VKVSYKGSPAARRAFLP-ILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 917
Cdd:PLN03142   246 RAVKFHGNPEERAHQREeLLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  918 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 997
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  998 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEESfsehlg 1076
Cdd:PLN03142   392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1077 ftGGIVQGSDLYRASGKFELLDRILPKLRATNHKVLLFCQMTTLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFND 1156
Cdd:PLN03142   458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1157 PSHQYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1236
Cdd:PLN03142   536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                   ....*...
gi 1207168553 1237 DQKVIQAG 1244
Cdd:PLN03142   616 DALVIQQG 623
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
743-993 1.25e-156

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: 476.48  E-value: 1.25e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  743 YYAVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIV 822
Cdd:cd18063      1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  823 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHH 902
Cdd:cd18063     81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  903 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 982
Cdd:cd18063    161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1207168553  983 VLRPFLLRRLK 993
Cdd:cd18063    241 VLRPFLLRRLK 251
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
546-1228 4.77e-122

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 399.21  E-value: 4.77e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  546 RRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRAHKAAQALKDKKKKKKKKKPENAEGGAPALGPDGEPLD 625
Cdd:COG0553     24 LRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  626 ETSQMSDLPVKVIHVDSGKILTGMDAPKAGQLDTWLEMNPGYEVAPRSDSEDSGSDEEEDDEEEPQPSQAPTEEKKVIPD 705
Cdd:COG0553    104 LALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  706 PDSEDVSEVDARHIIEHAKQDVDDEYGNSAFIRGLQSYYAVAHAVTEKVEKQSSLlvNGQLKQYQIKGLEWLVSLYNNNL 785
Cdd:COG0553    184 LALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  786 NGILADEMGLGKTIQTIALITYLMEfKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFLPIlrsGKF 865
Cdd:COG0553    262 GGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPF---EDA 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  866 NVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNThyL-APRRVLLTGTPLQNKLPELWALLNFLLPTI 944
Cdd:COG0553    338 DLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA--LkARHRLALTGTPVENRLEELWSLLDFLNPGL 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  945 FKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMq 1024
Cdd:COG0553    416 LGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV- 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1025 akgVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHlgftggivqgsdlyraSGKFELLDRILPKL 1104
Cdd:COG0553    485 ---LEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR----------------SAKLEALLELLEEL 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1105 RATNHKVLLFCQMTTLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFNDPShQYFIFLLSTRAGGLGLNLQSADTVI 1184
Cdd:COG0553    546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGP-EAPVFLISLKAGGEGLNLTAADHVI 624
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1207168553 1185 IFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1228
Cdd:COG0553    625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
769-1064 1.89e-112

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: 357.76  E-value: 1.89e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  769 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEFKRL-NGPFLIIVPLSTLSNWVYEFDKWA--PSVVKV 844
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  845 SYKGSPAARRAFLPIL-RSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRVLLTG 923
Cdd:pfam00176   81 VLHGNKRPQERWKNDPnFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  924 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 1003
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207168553 1004 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1064
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
763-993 3.94e-93

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: 300.39  E-value: 3.94e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  763 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVV 842
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  843 KVSYKGSPAARRAFL-PILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlaprR 918
Cdd:cd17997     81 VVVLIGDKEERADIIrDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVrlfNSRN----R 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168553  919 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNApfamtgEKVDLNEEEtilIIRRLHKVLRPFLLRRLK 993
Cdd:cd17997    157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV------NNCDDDNQE---VVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
763-993 2.05e-91

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: 296.22  E-value: 2.05e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  763 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEfKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVV 842
Cdd:cd18009      1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  843 KVSYKGSPAARRAFLPILRS-----GKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPR 917
Cdd:cd18009     80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168553  918 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN--APFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLK 993
Cdd:cd18009    159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
766-991 1.11e-80

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: 264.98  E-value: 1.11e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAflpiLRSG-----KFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNThYLAPRRVL 920
Cdd:cd18003     81 YYGSAKERKL----KRQGwmkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLL 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207168553  921 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF-AMTGEKVDLNEEetilIIRRLHKVLRPFLLRR 991
Cdd:cd18003    156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLtAMSEGSQEENEE----LVRRLHKVLRPFLLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
766-942 8.01e-79

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: 257.88  E-value: 8.01e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNTHYlAPRRVLLTGTP 925
Cdd:cd17919     81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159
                          170
                   ....*....|....*..
gi 1207168553  926 LQNKLPELWALLNFLLP 942
Cdd:cd17919    160 LQNNLEELWALLDFLDP 176
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
765-991 4.73e-78

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: 257.28  E-value: 4.73e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  765 QLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKV 844
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  845 SYKGSPAARRA------FLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNThYLAPRR 918
Cdd:cd17993     81 VYLGDIKSRDTireyefYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553  919 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgekVDLNEEETILiIRRLHKVLRPFLLRR 991
Cdd:cd17993    160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
766-991 3.21e-75

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: 249.47  E-value: 3.21e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVkVS 845
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMNV-VV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARR------------AFLPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNtHY 913
Cdd:cd17995     80 YHGSGESRQiiqqyemyfkdaQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168553  914 LAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 991
Cdd:cd17995    159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
753-1003 1.22e-73

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: 245.73  E-value: 1.22e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  753 KVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVY 832
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  833 EFDKWAPSVVKVSYKGSPAARRAFL-PILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNt 911
Cdd:cd18064     83 EFKRWVPTLRAVCLIGDKDQRAAFVrDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  912 HYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRR 991
Cdd:cd18064    162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRR 231
                          250
                   ....*....|..
gi 1207168553  992 LKKEVEAQLPEK 1003
Cdd:cd18064    232 IKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
753-993 2.91e-72

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: 241.46  E-value: 2.91e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  753 KVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVY 832
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  833 EFDKWAPSVVKVSYKGSPAARRAFL-PILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNt 911
Cdd:cd18065     83 EFKRWVPSLRAVCLIGDKDARAAFIrDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  912 HYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRR 991
Cdd:cd18065    162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 231

                   ..
gi 1207168553  992 LK 993
Cdd:cd18065    232 IK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
766-991 8.80e-64

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: 216.60  E-value: 8.80e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLPIL-------RSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 918
Cdd:cd18002     81 YWGNPKDRKVLRKFWdrknlytRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168553  919 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE-KVDLNEEEtiliIRRLHKVLRPFLLRR 991
Cdd:cd18002    160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAEnKTGLNEHQ----LKRLHMILKPFMLRR 229
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
762-993 1.15e-61

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: 210.11  E-value: 1.15e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  762 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEfKRLNGPFLIIVPLSTLSNWVYEFDKWAPSV 841
Cdd:cd18012      1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  842 VKVSYKGSPAARRAflpILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQV---LNTHYlaprR 918
Cdd:cd18012     80 KVLVIHGTKRKREK---LRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLKADH----R 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168553  919 VLLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGEKvDLNEEEtiliIRRLHKVLRPFLLRRLK 993
Cdd:cd18012    153 LALTGTPIENHLGELWSIFDFLNPGLLGS----YKRFKKRFAKPIEK-DGDEEA----LEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
754-991 2.64e-61

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: 209.86  E-value: 2.64e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  754 VEKQSSLL--VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWV 831
Cdd:cd18054      7 LKKQPSYIggENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  832 YEFDKWAPSVVKVSYKGSPAARRAFL------PILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKL 905
Cdd:cd18054     87 REFEIWAPEINVVVYIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  906 TQVLnTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLR 985
Cdd:cd18054    167 YKTL-IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLE 231

                   ....*.
gi 1207168553  986 PFLLRR 991
Cdd:cd18054    232 PFLLRR 237
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1440-1545 4.54e-61

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: 203.81  E-value: 4.54e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQT 81
                           90       100
                   ....*....|....*....|....*.
gi 1207168553 1520 FNLEGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:cd05516     82 FNLEGSLIYEDSIVLQSVFKSARQKI 107
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
766-991 3.67e-58

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: 199.97  E-value: 3.67e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLPILRS-GKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNTHYLaPRRVLLTGT 924
Cdd:cd18006     81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168553  925 PLQNKLPELWALLNFLLPTIFkSCSTFEQWFNApFAMTGEKVDLNEEetiliirrLHKVLRPFLLRR 991
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) ...
1091-1217 3.10e-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: 191.15  E-value: 3.10e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1091 SGKFELLDRILPKLRATNHKVLLFCQMTTLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFNDPShQYFIFLLSTRA 1170
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1207168553 1171 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1217
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; ...
766-991 2.51e-55

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


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 191.11  E-value: 2.51e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSpaarraflpilrsgkfNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNTHYLApRRVLLTGTP 925
Cdd:cd17994     81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207168553  926 LQNKLPELWALLNFLLPTIFKSCSTFeqwfnapfamTGEKVDLNEEETiliIRRLHKVLRPFLLRR 991
Cdd:cd17994    144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
766-945 7.12e-54

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: 186.82  E-value: 7.12e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRlNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLPILRSG--KFNVLVTTYEYII---KDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNThYLAPRRVL 920
Cdd:cd17998     80 YYGSQEERKHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INANFRLL 158
                          170       180
                   ....*....|....*....|....*
gi 1207168553  921 LTGTPLQNKLPELWALLNFLLPTIF 945
Cdd:cd17998    159 LTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
766-991 4.14e-51

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: 180.24  E-value: 4.14e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMeFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVs 845
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIV- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFL------------PILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNTHY 913
Cdd:cd18058     79 YHGSQISRQMIQqyemyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168553  914 LApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 991
Cdd:cd18058    159 LE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
766-942 1.65e-49

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: 174.43  E-value: 1.65e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAP------ 839
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  840 ------SVVKVSYKGSPAARRAFLPILRsGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQV---LN 910
Cdd:cd18000     81 lhssgsGTGSEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLR 159
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1207168553  911 ThylaPRRVLLTGTPLQNKLPELWALLNFLLP 942
Cdd:cd18000    160 T----PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
766-991 3.92e-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: 174.85  E-value: 3.92e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT---YL--MEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPS 840
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILAsdhHKraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  841 VVK--VSYKGSPAARRAFLPILrsGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 918
Cdd:cd17999     81 AFLkpLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANHR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207168553  919 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVD--LNEEETILIIRRLHKVLRPFLLRR 991
Cdd:cd17999    158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKAsaKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
765-991 1.85e-48

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: 173.31  E-value: 1.85e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  765 QLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKV 844
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  845 SYKGSPAARRAFL------PILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 918
Cdd:cd18053    100 VYLGDINSRNMIRthewmhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHR 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553  919 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 991
Cdd:cd18053    179 LLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
766-991 2.24e-48

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: 172.56  E-value: 2.24e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPfLIIVPLSTLSNWVYEFDKWAPSV-VKV 844
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLrVKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  845 SYKGSPAARRAFL-PILRsgKFNVLVTTYEYIIKDKQVLA-----KLRWKYMIVDEGHRMKNHHCKLTQVLntHYL-APR 917
Cdd:cd18001     80 FHGTSKKERERNLeRIQR--GGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAKN 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168553  918 RVLLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPFAMTGEKVDLNEEETI--LIIRRLHKVLRPFLLRR 991
Cdd:cd18001    156 RIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKALgsEVAENLRQIIKPYFLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
766-991 2.74e-47

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: 169.87  E-value: 2.74e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLM--------------EFKR------LNGPFLIIVPLS 825
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrpRFKKkppassAKKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  826 TLSNWVYEFDKWAPSVVKVsYKGSpaaRRAFLPILR--SGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHC 903
Cdd:cd18005     81 VLYNWKDELDTWGHFEVGV-YHGS---RKDDELEGRlkAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  904 KLTQVLNThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF----AMTGEKVDLNEEETilIIRR 979
Cdd:cd18005    157 KLTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK--RKQE 233
                          250
                   ....*....|..
gi 1207168553  980 LHKVLRPFLLRR 991
Cdd:cd18005    234 LAVKLSKFFLRR 245
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
766-991 3.32e-47

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: 169.08  E-value: 3.32e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKrLNGPFLIIVPLSTLSNWVYEFDKWApSVVKVS 845
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLP------------ILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNtHY 913
Cdd:cd18060     79 YHGSLASRQMIQQyemyckdsrgrlIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK-HM 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168553  914 LAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 991
Cdd:cd18060    158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
766-991 9.55e-47

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: 167.52  E-value: 9.55e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVkVS 845
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV-VV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLP------------ILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNTHY 913
Cdd:cd18059     79 YHGSQASRRTIQLyemyfkdpqgrvIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168553  914 LApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 991
Cdd:cd18059    159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
766-991 2.36e-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: 166.73  E-value: 2.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAAR-------------------RAF-LPILRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKL 905
Cdd:cd18055     81 YTGDKDSRaiirenefsfddnavkggkKAFkMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  906 TQVLNThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 985
Cdd:cd18055    161 FRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                   ....*.
gi 1207168553  986 PFLLRR 991
Cdd:cd18055    227 PHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
766-991 3.58e-46

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: 166.39  E-value: 3.58e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLP--------ILRSG------------KFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKL 905
Cdd:cd18057     81 YTGDKESRSVIREnefsfednAIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  906 TQVLNThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 985
Cdd:cd18057    161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                   ....*.
gi 1207168553  986 PFLLRR 991
Cdd:cd18057    227 PHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
766-991 1.90e-43

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: 158.69  E-value: 1.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 845
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  846 YKGSPAARRAFLP--------ILRSG------------KFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKL 905
Cdd:cd18056     81 YVGDKDSRAIIREnefsfednAIRGGkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  906 TQVLNTHYLApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 985
Cdd:cd18056    161 FRVLNGYSLQ-HKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDMLG 226

                   ....*.
gi 1207168553  986 PFLLRR 991
Cdd:cd18056    227 PHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
766-991 2.06e-43

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: 157.86  E-value: 2.06e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTialITYLMEFKR--LNGPFLIIVPLSTLSNWVYEFDKWAPSVVk 843
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS---ITFLYEILLtgIRGPFLIIAPLSTIANWEREFRTWTDLNV- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  844 VSYKGSPAARRAFLP-----------ILRSG-KFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNT 911
Cdd:cd18061     77 VVYHGSLISRQMIQQyemyfrdsqgrIIRGAyRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  912 HYLApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 991
Cdd:cd18061    157 MNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
766-991 3.33e-41

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: 152.44  E-value: 3.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVS--LYNNNLNG---ILADEMGLGKTIQTIALITYLMEFKRLNGP----FLIIVPLSTLSNWVYEFDK 836
Cdd:cd18004      1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  837 WAPSVVK--VSYKGSPAARRAFLPILRSGK-FNVLVTTYEYIIKDKQVLAKL-RWKYMIVDEGHRMKNHHCKLTQVLNTh 912
Cdd:cd18004     81 WLGLRRIkvVTADGNAKDVKASLDFFSSAStYPVLIISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSESKTTKALNS- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  913 YLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvDLNEEETILIIRRLH---KVLRPFLL 989
Cdd:cd18004    160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRFIL 238

                   ..
gi 1207168553  990 RR 991
Cdd:cd18004    239 RR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
766-991 9.84e-40

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: 148.20  E-value: 9.84e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLynnnlNGILADEMGLGKTIQTIALI-----------------TYLMEFKRLNGPFLIIVPLSTLS 828
Cdd:cd18008      1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeeleenSSDPKKLYLSKTTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  829 NWVYEFDK-WAPSVVKVS-YKGSPaaRRAFLPILRSgkFNVLVTTY-----EY-----------IIKDKQVLAKLRWKYM 890
Cdd:cd18008     76 QWKDEIEKhTKPGSLKVYvYHGSK--RIKSIEELSD--YDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWYRV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  891 IVDEGHRMKNHHCKLTQV---LNTHylapRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvd 967
Cdd:cd18008    152 ILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225
                          250       260
                   ....*....|....*....|....
gi 1207168553  968 lneeetilIIRRLHKVLRPFLLRR 991
Cdd:cd18008    226 --------ALERLQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
766-979 3.20e-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: 137.81  E-value: 3.20e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLE--W--LVSLYNNNLNG---ILADEMGLGKTIQTIALI-TYLMEFKRLNGPfLIIVPLSTLSNWVYEFDKW 837
Cdd:cd18007      1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  838 APSVVK----VSYKGSPAARRAFLPILRSGKFN--VLVTTYEY---IIKDKQVLAKLRWKYM-----------IVDEGHR 897
Cdd:cd18007     80 LPPDLRpllvLVSLSASKRADARLRKINKWHKEggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEGHR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  898 MKNHHCKLTQVLNTHYlAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILII 977
Cdd:cd18007    160 LKNEKSQLSKALSKVK-TKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIE-AGQCVDSTEEDVRLML 237

                   ..
gi 1207168553  978 RR 979
Cdd:cd18007    238 KR 239
DEXDc smart00487
DEAD-like helicases superfamily;
765-954 3.43e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.22  E-value: 3.43e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   765 QLKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEFKrlNGPFLIIVPLSTL-SNWVYEFDKWAPS-V 841
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   842 VKVSYKGSPAARRAFLPILRSGKFNVLVTTYEYIIKD--KQVLAKLRWKYMIVDEGHRMKN--HHCKLTQVLNTHYLAPR 917
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1207168553   918 RVLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 954
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1440-1543 8.53e-31

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: 117.41  E-value: 8.53e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05515      1 MQQKLWELYNAVKNYTDGRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACK 80
                           90       100
                   ....*....|....*....|....
gi 1207168553 1520 FNLEGSLIYEDSIVLQSVFTSVRQ 1543
Cdd:cd05515     81 YNEPDSQIYKDALTLQKVLLETKR 104
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
766-991 3.72e-30

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: 120.27  E-value: 3.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNL-----------------------------NGILADEMGLGKTIQTIALItylmefkrLNG 816
Cdd:cd18071      1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LAN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  817 PFLIIVPLSTLSNWVYEF-DKWAPSVVKV-SYKGSPAARRA-FLpilrsGKFNVLVTTY-----EYIIKDKQVLAKLRWK 888
Cdd:cd18071     73 FTLIVCPLSVLSNWETQFeEHVKPGQLKVyTYHGGERNRDPkLL-----SKYDIVLTTYntlasDFGAKGDSPLHTINWL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  889 YMIVDEGHRMKNHHCKLTQ-VLNTHylAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVD 967
Cdd:cd18071    148 RVVLDEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTG 224
                          250       260
                   ....*....|....*....|....
gi 1207168553  968 LneeetiliiRRLHKVLRPFLLRR 991
Cdd:cd18071    225 L---------KRLQVLMKQITLRR 239
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
766-991 3.83e-29

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: 117.25  E-value: 3.83e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSL-----YNNNLNGILADEMGLGKTIQTIALITYLME-----FKRLNGPFLIIVPLSTLSNWVYEFD 835
Cdd:cd18066      1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRqgpygGKPVIKRALIVTPGSLVKNWKKEFQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  836 KWAPSV-VKVSYKGSPAARRAFLpilRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLnTHYL 914
Cdd:cd18066     81 KWLGSErIKVFTVDQDHKVEEFI---ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL-TSLS 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553  915 APRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIR--RLHKVLRPFLLRR 991
Cdd:cd18066    157 CERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTRLTGLFILRR 235
BROMO smart00297
bromo domain;
1438-1545 1.02e-28

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 111.60  E-value: 1.02e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  1438 PSLTKKMKKTVDAVIKYKDGngRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNA 1517
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|....*...
gi 1207168553  1518 QTFNLEGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1092-1206 1.11e-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: 111.53  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1092 GKFELLDRILPKLRatNHKVLLFCQMTTlmTIMEDYFAYR-NFKYLRLDGTTKAEDRGMLLKNFNDPSHQyfiFLLSTRA 1170
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1207168553 1171 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1206
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1440-1541 5.40e-28

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: 109.35  E-value: 5.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05519      1 LKAAMLEIYDAVLNCEDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANART 80
                           90       100
                   ....*....|....*....|..
gi 1207168553 1520 FNLEGSLIYEDSIVLQSVFTSV 1541
Cdd:cd05519     81 YNQEGSIVYEDAVEMEKAFKKK 102
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
766-991 1.32e-27

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: 113.33  E-value: 1.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLM----EFKRLNGPFLIIVPLSTLSNWVYEFDK 836
Cdd:cd18067      1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  837 W-APSVVKVSYKG--------------SPAARRAFLPilrsgkfnVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNH 901
Cdd:cd18067     81 WlGGRLQPLAIDGgskkeidrklvqwaSQQGRRVSTP--------VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  902 HCKLTQVLNThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLH 981
Cdd:cd18067    153 DNQTYQALDS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPI-LKGRDADASEKERQLGEEKLQ 230
                          250
                   ....*....|...
gi 1207168553  982 K---VLRPFLLRR 991
Cdd:cd18067    231 ElisIVNRCIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
766-979 1.78e-27

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: 111.91  E-value: 1.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSlynNNLNGILADEMGLGKTIQTIALITYLmefkRLNGPFLIIVPLSTLSNWVYEFDKWAPSV---- 841
Cdd:cd18010      1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLppdd 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  842 VKVSYKGSPAarraflpiLRSGKFNVLVTTYEYIIKDKQVLAKLRWKYMIVDEGHRMKNHHCKLTQV---LNTHylAPRR 918
Cdd:cd18010     74 IQVIVKSKDG--------LRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRV 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  919 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTF-EQWFNA----PFAMTGEKVDLNEEETILI----IRR 979
Cdd:cd18010    144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgRRYCAAkqggFGWDYSGSSNLEELHLLLLatimIRR 213
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1440-1538 6.83e-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: 105.92  E-value: 6.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKdgngRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd04369      1 LKKKLRSLLDALKKLK----RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKT 76
                           90
                   ....*....|....*....
gi 1207168553 1520 FNLEGSLIYEDSIVLQSVF 1538
Cdd:cd04369     77 YNGPGSPIYKDAKKLEKLF 95
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1442-1537 3.82e-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: 101.37  E-value: 3.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1442 KKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFN 1521
Cdd:cd05518      3 KRMLALFLYVLEYREGSGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYN 82
                           90
                   ....*....|....*.
gi 1207168553 1522 LEGSLIYEDSIVLQSV 1537
Cdd:cd05518     83 EEGSQVYEDANILEKV 98
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
766-979 3.54e-24

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: 102.59  E-value: 3.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEFKRLNgPFLIIVPLSTLSNWVYE 833
Cdd:cd18069      1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  834 FDKWAPSVVKVSyKGSPAARRAFLPILRSGKFNVLVTTYEYIIKDKQVLA------KLR--WKYMIVDEGHRMKNHHCKL 905
Cdd:cd18069     77 FNKWLPPPEALP-NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLmgyemfRLRpgPDVVICDEGHRIKNCHAST 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168553  906 TQVLNtHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR 979
Cdd:cd18069    156 SQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCVDSTPQDVKLMRYR 227
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1301-1368 1.37e-23

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: 95.40  E-value: 1.37e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1301 DRRREEARNPK-RRPRLMEEDELPTWIMKDDAEVERLTCEEEEEKMFGRGSRQRKEVDYSDSLTEKQWL 1368
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
478-550 2.10e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.16  E-value: 2.10e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553   478 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 550
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1448-1539 2.14e-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: 96.35  E-value: 2.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1448 VDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLI 1527
Cdd:cd05517      9 LEAVMTATDPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQV 88
                           90
                   ....*....|..
gi 1207168553 1528 YEDSIVLQSVFT 1539
Cdd:cd05517     89 YKDANAIKKIFT 100
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1448-1545 2.66e-22

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: 93.55  E-value: 2.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1448 VDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLI 1527
Cdd:cd05524     11 YDTIRNYKSEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPE 90
                           90
                   ....*....|....*...
gi 1207168553 1528 YEDSIVLQSVFTSVRQKI 1545
Cdd:cd05524     91 HKDACKLWELFLSARNEV 108
HELICc smart00490
helicase superfamily c-terminal domain;
1123-1206 4.51e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 4.51e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  1123 IMEDYFAYRNFKYLRLDGTTKAEDRGMLLKNFNDPShqyFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1202
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK---IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1207168553  1203 HRIG 1206
Cdd:smart00490   79 GRAG 82
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
479-545 6.16e-21

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


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 88.01  E-value: 6.16e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168553  479 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQKKENERIEKERM 545
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
766-991 1.19e-20

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: 92.93  E-value: 1.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTIALITY----------------LMEFKRLN------GPFLIIV 822
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAqkntqnrkeeekekalTEWESKKDstlvpsAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  823 PLSTLSNWVYEFD-KWAPSVVKV-SYKGSPAARRAflPILRSgkFNVLVTTYEYIIK----DKQ-----VLAKLRWKYMI 891
Cdd:cd18072     81 PASLVHQWKNEVEsRVASNKLRVcLYHGPNRERIG--EVLRD--YDIVITTYSLVAKeiptYKEesrssPLFRIAWARII 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  892 VDEGHRMKNHH-------CKLtqvlNTHYlaprRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE 964
Cdd:cd18072    157 LDEAHNIKNPKvqasiavCKL----RAHA----RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGE 228
                          250       260
                   ....*....|....*....|....*..
gi 1207168553  965 kvdlneeetiliirRLHKVLRPFLLRR 991
Cdd:cd18072    229 --------------RLNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
787-979 1.88e-20

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: 92.64  E-value: 1.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  787 GILADEMGLGKTIQTIALI-TYLMEFKRLN-GPFLIIVPLSTLSNWVYEFDKWA-----PSVVKV----SYKGSPaaRRA 855
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLhTVLLCEKLENfSRVLVVCPLNTVLNWLNEFEKWQeglkdEEKIEVnelaTYKRPQ--ERS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  856 FLPILRSGKFNVLVTTYE-YII----KDKQVLAKLRWKYM-----------IVDEGHRMKNHHCKLTQVLNThYLAPRRV 919
Cdd:cd18068    109 YKLQRWQEEGGVMIIGYDmYRIlaqeRNVKSREKLKEIFNkalvdpgpdfvVCDEGHILKNEASAVSKAMNS-IRTKRRI 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  920 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILIIRR 979
Cdd:cd18068    188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NGQCADSTLVDVRVMKKR 246
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1459-1537 1.77e-19

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: 85.08  E-value: 1.77e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1459 GRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSV 1537
Cdd:cd05520     20 GQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQKL 98
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
788-945 9.39e-19

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: 86.57  E-value: 9.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  788 ILADEMGLGKTIQTIALITYLMeFKRLNGPFLIIVPLSTLSNW-VYEFDK-WAPSVVKVSYKGSPAARRAFLPILRsgkF 865
Cdd:cd18011     21 LLADEVGLGKTIEAGLIIKELL-LRGDAKRVLILCPASLVEQWqDELQDKfGLPFLILDRETAAQLRRLIGNPFEE---F 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  866 NVLVTTYEYI---IKDKQVLAKLRWKYMIVDEGHRMKNHHC-------KLTQVLNTHylAPRRVLLTGTPLQNKLPELWA 935
Cdd:cd18011     97 PIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEEDFRA 174
                          170
                   ....*....|
gi 1207168553  936 LLNFLLPTIF 945
Cdd:cd18011    175 LLSLLDPGRF 184
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1460-1531 2.25e-18

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: 81.21  E-value: 2.25e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207168553 1460 RQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDS 1531
Cdd:pfam00439   11 HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAA 82
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1440-1536 8.85e-18

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: 80.44  E-value: 8.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRshKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05521      2 LSKKLKPLYDGIYTLKEENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLAQIPWNARL 79
                           90
                   ....*....|....*..
gi 1207168553 1520 FNLEGSLIYEDSIVLQS 1536
Cdd:cd05521     80 YNTKGSVIYKYALILEK 96
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1453-1541 2.73e-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: 78.82  E-value: 2.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1453 KYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSI 1532
Cdd:cd05522     15 KERDENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAV 94

                   ....*....
gi 1207168553 1533 VLQSVFTSV 1541
Cdd:cd05522     95 LLEKEARLL 103
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1428-1545 6.71e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.39  E-value: 6.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1428 PPAEKLSPNPPS---LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLN 1504
Cdd:COG5076    128 TSVKKRKTPKIEdelLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFE 207
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1207168553 1505 DLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:COG5076    208 EFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEI 248
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
629-672 1.44e-15

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: 71.77  E-value: 1.44e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1207168553  629 QMSDLPVKVIHVDSGKILTGMDAPKAGQLDTWLEMNPGYEVAPR 672
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
766-956 1.66e-15

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: 77.39  E-value: 1.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVSlynNNLNGILADeMGLGKTIQTIALITYLMeFKRLNGPFLIIVPLSTLSN-WVYEFDKW-APSVVK 843
Cdd:cd18013      1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWnHLRNLT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  844 VSYK-GSPAARRAFLpilrSGKFNVLVTTYEYIIK-DKQVLAKLRWKYMIVDEGHRMKNHHCKLTQVLNTH-YLAPRRVL 920
Cdd:cd18013     76 VSVAvGTERQRSKAA----NTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKRLIG 151
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1207168553  921 LTGTPLQNKLPELWALLNFL--LPTIFKSCSTF-EQWFN 956
Cdd:cd18013    152 LTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
766-940 8.26e-14

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: 73.15  E-value: 8.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLEWLVslynnNLNGILADEMGLGKTIQTIALI------------TYLMEFKRLN-------------GPFLI 820
Cdd:cd18070      1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCcpdclvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  821 IVPLSTLSNWVYEFDKWAPSVVKVS-YKG---SPAARRAFLPILRSgkFNVLVTTYEYIIKD------------------ 878
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLtYQGvkkDGALASPAPEILAE--YDIVVTTYDVLRTElhyaeanrsnrrrrrqkr 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168553  879 ----KQVLAKLRWKYMIVDEghrMKNHHCKLTQVLNTHYLAPR--RVLLTGTPLQNKLPELWALLNFL 940
Cdd:cd18070    154 yeapPSPLVLVEWWRVCLDE---AQMVESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFL 218
BRK smart00592
domain in transcription and CHROMO domain helicases;
630-672 9.52e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 66.60  E-value: 9.52e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1207168553   630 MSDLPVKVIHVDSGKILTGMDAPKAGQLDTWLEMNPGYEVAPR 672
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 ...
198-231 5.64e-13

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: 64.28  E-value: 5.64e-13
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207168553  198 FNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 231
Cdd:pfam08880    2 FTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1440-1543 2.17e-12

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: 65.10  E-value: 2.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAVIKYKDGNGRQLSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05525      3 LAQVLKEICDAIITYKDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEK 82
                           90       100
                   ....*....|....*....|....
gi 1207168553 1520 FNLEGSLIYEDSIVLQSVFTSVRQ 1543
Cdd:cd05525     83 YYGRKSPIGRDVCRLRKAYYQAKH 106
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1466-1538 6.75e-12

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: 63.34  E-value: 6.75e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553 1466 FIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1538
Cdd:cd05509     22 FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTEYYKCANKLEKFF 94
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1448-1538 9.10e-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: 63.57  E-value: 9.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1448 VDAVIKYKDgngrqlSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLI 1527
Cdd:cd05504     21 LVEIVKHKD------SWPFLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSV 94
                           90
                   ....*....|.
gi 1207168553 1528 YEDSIVLQSVF 1538
Cdd:cd05504     95 YKAGTRLQRFF 105
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
786-924 2.75e-11

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: 63.19  E-value: 2.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  786 NGILADEMGLGKTIqtIALITYLMEFKRLNGPFLIIVPLSTLSNWVYE-FDKWAPSVVKVSY--KGSPAARRAFLPILRS 862
Cdd:cd00046      3 NVLITAPTGSGKTL--AALLAALLLLLKKGKKVLVLVPTKALALQTAErLRELFGPGIRVAVlvGGSSAEEREKNKLGDA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553  863 gkfNVLVTTYEYIIKDKQVLAKL---RWKYMIVDEGHRM----KNHHCKLTQVLNTHYLAPRRVLLTGT 924
Cdd:cd00046     81 ---DIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1470-1538 7.23e-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: 60.38  E-value: 7.23e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1470 PSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1538
Cdd:cd05499     30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVF 98
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1474-1521 9.42e-11

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: 60.45  E-value: 9.42e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207168553 1474 ELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFN 1521
Cdd:cd05528     32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
198-230 3.20e-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: 56.39  E-value: 3.20e-10
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1207168553   198 FNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 230
Cdd:smart00951    3 FTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
ResIII pfam04851
Type III restriction enzyme, res subunit;
765-925 8.14e-10

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 59.22  E-value: 8.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  765 QLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEfKRLNGPFLIIVP-LSTLSNWVYEFDKWAPSVV 842
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  843 KVSYKGSPaarRAFLPILRSGKfnVLVTTYEYIIKD----KQVLAKLRWKYMIVDEGHRM--KNHhcklTQVLNthYLAP 916
Cdd:pfam04851   82 EIGEIISG---DKKDESVDDNK--IVVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE--YFKP 150
                          170
                   ....*....|
gi 1207168553  917 RRVL-LTGTP 925
Cdd:pfam04851  151 AFLLgLTATP 160
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1440-1535 1.45e-09

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: 56.64  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1440 LTKKMKKTVDAViKYKDGNgrqlsEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQT 1519
Cdd:cd05512      2 LEVLLRKTLDQL-QEKDTA-----EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLA 75
                           90
                   ....*....|....*.
gi 1207168553 1520 FNLEGSLIYEDSIVLQ 1535
Cdd:cd05512     76 YNAKDTIFYRAAVRLR 91
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
766-925 2.95e-09

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: 57.32  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  766 LKQYQIKGLE-WLvsLYNNNLNGILADEMGLGKTIQTIALITYLMEFKrlngpFLIIVP-LSTLSNWVYEFDKWAPSVVk 843
Cdd:cd17926      1 LRPYQEEALEaWL--AHKNNRRGILVLPTGSGKTLTALALIAYLKELR-----TLIVVPtDALLDQWKERFEDFLGDSS- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  844 vsykgspaarrafLPILRSGK------FNVLVTTYEYIIKDKQVLAKL--RWKYMIVDEGHrmknHHC--KLTQVLnTHY 913
Cdd:cd17926     73 -------------IGLIGGGKkkdfddANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KEL 134
                          170
                   ....*....|..
gi 1207168553  914 LAPRRVLLTGTP 925
Cdd:cd17926    135 NAKYRLGLTATP 146
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1470-1539 1.33e-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: 54.21  E-value: 1.33e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1470 PSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFT 1539
Cdd:cd05498     30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1473-1540 1.61e-08

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: 53.53  E-value: 1.61e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207168553 1473 KELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1540
Cdd:cd05503     28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
382-624 1.63e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  382 VEILQEREY-------RLQARIAHRIQELENLPGSLAgdlRTKANIELKALRLLNFQRQLRQEvvvcmrrDTALETALNA 454
Cdd:COG1196    283 LEEAQAEEYellaelaRLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEEL-------EEELEEAEEE 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  455 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQK 534
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  535 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQALKDKKKKKKKKKPENAEGGA 614
Cdd:COG1196    433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
                          250
                   ....*....|
gi 1207168553  615 PALGPDGEPL 624
Cdd:COG1196    512 AALLLAGLRG 521
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1442-1545 2.48e-08

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: 53.62  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1442 KKMKKTVDAVIKYKDgngrqlSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFN 1521
Cdd:cd05496      8 KQCKELVNLMWDCED------SEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYT 81
                           90       100
                   ....*....|....*....|....*
gi 1207168553 1522 L-EGSLIYEDSIVLQSVFTSVRQKI 1545
Cdd:cd05496     82 PnKRSRIYSMTLRLSALFEEHIKKI 106
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1476-1528 3.73e-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: 52.80  E-value: 3.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207168553 1476 PEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIY 1528
Cdd:cd05513     32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYY 84
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1469-1540 4.97e-08

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: 53.11  E-value: 4.97e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207168553 1469 LPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1540
Cdd:cd05529     52 VDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWLLR 123
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1460-1545 6.45e-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: 52.29  E-value: 6.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1460 RQLSEVFIQLPSR-------KELPEYYELIRKPVDFRKIKERIR---SHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYE 1529
Cdd:cd05502     11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQ 90
                           90
                   ....*....|....*.
gi 1207168553 1530 DSIVLQSVFTSVRQKI 1545
Cdd:cd05502     91 AGKELELFFEEQLKEI 106
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1473-1545 1.11e-07

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: 51.88  E-value: 1.11e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207168553 1473 KELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNleGSliyedsivlQSVFTSVRQKI 1545
Cdd:cd05511     28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYN--GP---------DSVYTKKAKEM 89
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1470-1538 2.44e-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: 50.39  E-value: 2.44e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1470 PSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1538
Cdd:cd05500     31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
763-925 1.01e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 53.49  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  763 NGQLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEFKRLngpfLIIVPLSTLSN-WVYEFDKWAPS 840
Cdd:COG1061     78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  841 VVKVSYKgspaarraflpilRSGKFNVLVTTYEYIIKDKQvLAKL--RWKYMIVDEGhrmknHHC---KLTQVLNtHYLA 915
Cdd:COG1061    154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEA-----HHAgapSYRRILE-AFPA 213
                          170
                   ....*....|
gi 1207168553  916 PRRVLLTGTP 925
Cdd:COG1061    214 AYRLGLTATP 223
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
65-360 1.47e-06

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: 53.09  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   65 PQDNMHQMHKPMEGMHEKGIPEDQRYGQMKGMGMRQGGHSGMGPPPS---PMDQHSQGYPSPLGGSDHAPSPVPANGPPS 141
Cdd:pfam09606  151 PGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGgqmPPQMGVPGMPGPADAGAQMGQQAQANGGMN 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  142 GPMMPSGPGAMPMEGGDPQAMAQQNR--------------SGGAGGVAGPGpsggppnaggpggaggptpfNQNQLHQLR 207
Cdd:pfam09606  231 PQQMGGAPNQVAMQQQQPQQQGQQSQlgmginqmqqmpqgVGGGAGQGGPG--------------------QPMGPPGQQ 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  208 AQIMAYKMLARGQPLPDHLQMAVQGKR---PMPGMQQGMPNMP--PASGQGAGPPGPGVPGPGGPNY----------NRP 272
Cdd:pfam09606  291 PGAMPNVMSIGDQNNYQQQQTRQQQQQqggNHPAAHQQQMNQSvgQGGQVVALGGLNHLETWNPGNFgglganpmqrGQP 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  273 HGMVGPNMPPPGPSGVPPGLQGQPTNGPPK-PWPEGPMVNaaAPASAPQKLIPPqPTGRPSPAPPSVPPAASPVMPPQtQ 351
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQPSvPSPQGPGSQ--PPQSHPGGMIPS-PALIPSPSPQMSQQPAQQRTIGQ-D 446

                   ....*....
gi 1207168553  352 SPGQPAQPP 360
Cdd:pfam09606  447 SPGGSLNTP 455
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1470-1538 1.88e-06

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: 47.71  E-value: 1.88e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1470 PSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1538
Cdd:cd05506     27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIF 95
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1474-1545 6.19e-06

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: 46.65  E-value: 6.19e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207168553 1474 ELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGsliyeDSIVL--QSVFTSVRQKI 1545
Cdd:cd05497     36 NLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPG-----DDVVLmaQTLEKLFLQKL 104
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1451-1527 7.44e-06

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: 45.99  E-value: 7.44e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168553 1451 VIKYKDgngrqlSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLI 1527
Cdd:cd05505     12 ILKYRF------SWPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYYENGSYV 82
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
1450-1545 1.30e-05

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


Pssm-ID: 99956  Cd Length: 110  Bit Score: 45.82  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1450 AVIKYKDGNGRQLSEVFIQLPSRKELPEyyELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYE 1529
Cdd:cd05526     14 SVMNHQDEEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSEIYE 91
                           90
                   ....*....|....*.
gi 1207168553 1530 DSIVLQSVFTSVRQKI 1545
Cdd:cd05526     92 DAVELQQFFIKIRDEL 107
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
794-925 1.68e-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: 46.85  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  794 GLGKTIqtIALITYLMEFKRLNGPF--LIIVPLSTLSNWVYE-FDKWA-PSVVKVSYKGSPAARRAFLPILRSGkfNVLV 869
Cdd:pfam00270   24 GSGKTL--AFLLPALEALDKLDNGPqaLVLAPTRELAEQIYEeLKKLGkGLGLKVASLLGGDSRKEQLEKLKGP--DILV 99
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207168553  870 TTYE---YIIKDKQVLAKLrwKYMIVDEGHRM--KNHHCKLTQVLNTHYLAPRRVLLTGTP 925
Cdd:pfam00270  100 GTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1463-1521 2.12e-05

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


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 45.12  E-value: 2.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553 1463 SEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFN 1521
Cdd:cd05510     26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
794-893 2.29e-05

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: 46.94  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  794 GLGKTiqTIALITYLMeFKRLNGPFLIIVPLSTLSNWVYE----FDKWAPSVVK--VSYKGSPA-ARRAFLPILRSGKFN 866
Cdd:cd17924     42 GVGKT--TFGLATSLY-LASKGKRSYLIFPTKSLVKQAYErlskYAEKAGVEVKilVYHSRLKKkEKEELLEKIEKGDFD 118
                           90       100
                   ....*....|....*....|....*..
gi 1207168553  867 VLVTTYEYIIKDKQVLAKLRWKYMIVD 893
Cdd:cd17924    119 ILVTTNQFLSKNFDLLSNKKFDFVFVD 145
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1463-1521 2.48e-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: 44.66  E-value: 2.48e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1463 SEVFIQ-LPSRKElPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFN 1521
Cdd:cd05507     21 ASVFLKpVTEDIA-PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1160-1207 3.75e-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: 43.46  E-value: 3.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207168553 1160 QYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQ 1207
Cdd:cd18785     21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1470-1540 1.72e-04

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: 42.43  E-value: 1.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207168553 1470 PSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1540
Cdd:cd05495     31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQ 101
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
55-156 2.37e-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: 45.19  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553   55 PLPPQG----PSGYPQDNMHQM--HKPMEGMHEKGIPEDQRYGQM-KGMGMRQGGHSGMGPPPSPMDQHsqgypsPLGGS 127
Cdd:pfam15279  173 LLGKPQqhppPSPLPAFMEPSSmpPPFLRPPPSIPQPNSPLSNPMlPGIGPPPKPPRNLGPPSNPMHRP------PFSPH 246
                           90       100
                   ....*....|....*....|....*....
gi 1207168553  128 dHAPSPVPANGPPSGPMMPSGPGAMPMEG 156
Cdd:pfam15279  247 -HPPPPPTPPGPPPGLPPPPPRGFTPPFG 274
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
418-594 9.66e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 9.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  418 ANIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKaykrskRQSLREARiTEKLEKQQKIEQERKRRQKHQEYLNSI 497
Cdd:COG1579     13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAA------KTELEDLE-KEIKRLELEIEEVEARIKKYEEQLGNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  498 lqhaKDFKEYhrsitakmQKLTKAVATyhantereQKKENERIEKErMRRLMAEDEEgYRKLIDQKKDK------RLAYL 571
Cdd:COG1579     86 ----RNNKEY--------EALQKEIES--------LKRRISDLEDE-ILELMERIEE-LEEELAELEAElaeleaELEEK 143
                          170       180
                   ....*....|....*....|...
gi 1207168553  572 LQQTDEYVANLTELVRAHKAAQA 594
Cdd:COG1579    144 KAELDEELAELEAELEELEAERE 166
PTZ00121 PTZ00121
MAEBL; Provisional
455-566 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  455 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHAntEREQK 534
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207168553  535 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 566
Cdd:PTZ00121  1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
385-594 1.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  385 LQEREYRLQARIAHRIQELENLpgslagdLRTKANIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQS 464
Cdd:COG1196    237 LEAELEELEAELEELEAELEEL-------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  465 LREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHAN---TEREQKKENERIE 541
Cdd:COG1196    310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaeAEEELEELAEELL 389
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207168553  542 KERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRAHKAAQA 594
Cdd:COG1196    390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
406-616 2.54e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  406 LPGSLAGDLRTKANIELKALR-----LLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKI 480
Cdd:COG4942     13 LAAAAQADAAAEAEAELEQLQqeiaeLEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  481 EQERKRRQKHQEYLNSILQ---------------HAKDFKE------YHRSITAKMQKLTKAVATyhANTEREQKKENER 539
Cdd:COG4942     93 AELRAELEAQKEELAELLRalyrlgrqpplalllSPEDFLDavrrlqYLKYLAPARREQAEELRA--DLAELAALRAELE 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207168553  540 IEKERMRRLMAEDEEGYRKLIDQKKDKR--LAYLLQQTDEYVANLTELVRAHKAAQALKDKKKKKKKKKPENAEGGAPA 616
Cdd:COG4942    171 AERAELEALLAELEEERAALEALKAERQklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
383-568 4.52e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  383 EILQEREyRLQARIAHRIQELEnlpgslagdlRTKANIElkALRLlnfqrQLRQEVVVCMRRDTALETALNakayKRSKR 462
Cdd:pfam13868  177 EIEEEKE-REIARLRAQQEKAQ----------DEKAERD--ELRA-----KLYQEEQERKERQKEREEAEK----KARQR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  463 QSLREARiteKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANT--EREQKKENERI 540
Cdd:pfam13868  235 QELQQAR---EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieEREEQRAAERE 311
                          170       180
                   ....*....|....*....|....*...
gi 1207168553  541 EKERMRRLMAEDEEGYRKLIDQKKDKRL 568
Cdd:pfam13868  312 EELEEGERLREEEAERRERIEEERQKKL 339
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1439-1525 6.12e-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: 37.75  E-value: 6.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553 1439 SLTKKMKKTVDAVIKYKdgngrqlSEVFIQLPSRKELPEYYELIRKPVDFRKIKERIRSHKYRSLNDLEKDVMLLCQNAQ 1518
Cdd:cd05508      3 QLSKLLKFALERMKQPG-------AEPFLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAI 75

                   ....*..
gi 1207168553 1519 TFNLEGS 1525
Cdd:cd05508     76 IYNGGDH 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
394-594 6.41e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  394 ARIAHRIQELE-NLpgslaGDLRTKANIELKALRLLNFQRQLRQEVVVcmRRDTALETALNAKAYKRSKRQSLREARITE 472
Cdd:COG1196    189 ERLEDILGELErQL-----EPLERQAEKAERYRELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAE 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  473 KLEKQQKIEQERkrrQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMAED 552
Cdd:COG1196    262 LAELEAELEELR---LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1207168553  553 EEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQA 594
Cdd:COG1196    339 LEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEE 379
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
447-594 6.57e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  447 ALETALNAKAYKRSKRQSLREARitEKLEKQQK-IEQERKRRQKHQEYLNSILQHAKDFKEYHR------SITAKMQKLT 519
Cdd:COG4717     75 ELEEELKEAEEKEEEYAELQEEL--EELEEELEeLEAELEELREELEKLEKLLQLLPLYQELEAleaelaELPERLEELE 152
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207168553  520 KAVATYHANTEREQKKENERIEKER-MRRLMAEDEEGYRKLIdQKKDKRLAYLLQQTDEYVANLTELVRAHKAAQA 594
Cdd:COG4717    153 ERLEELRELEEELEELEAELAELQEeLEELLEQLSLATEEEL-QDLAEELEELQQRLAELEEELEEAQEELEELEE 227
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
431-577 6.93e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  431 QRQLRQEVvvcMRRDTALETALNAKAYKRSKRQSLREARITEklEKQQKIEQERKRRQKHQEYLNSILQHAKdfkEYHRS 510
Cdd:pfam15709  360 QRRLQQEQ---LERAEKMREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQLQAAQERARQQQE---EFRRK 431
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207168553  511 ITAKMQKLTKAVATyHANTEREQKKENERIEKERMRRLMAEDEEgyrklidqkkdKRLAYLLQQTDE 577
Cdd:pfam15709  432 LQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKRLMEMAEE-----------ERLEYQRQKQEA 486
PHA03247 PHA03247
large tegument protein UL36; Provisional
107-381 8.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 8.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  107 GPPPSPMDQHSQGYP--SPLGGSDHAPSPvPANGPPSGPmmPSGPGAMPMEGGDPQAMAQQNRSGGAGGVAGPGPSGGPP 184
Cdd:PHA03247  2590 DAPPQSARPRAPVDDrgDPRGPAPPSPLP-PDTHAPDPP--PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  185 NAGGPGGAGGPTPFNQNQLHQLRAQIMAYKMLARGQPlpdhlqmavQGKRPMPGMQQGMPNMPPASGQGAGPPGPGVPGP 264
Cdd:PHA03247  2667 ARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP---------PPPTPEPAPHALVSATPLPPGPAAARQASPALPA 2737
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  265 GGPNYNRPHGMVGPNMPPPGPSGvppglqgQPTNGPPKPWPegpmvnAAAPASAPQKLIPPQPTGRPSPAPpsvppaasp 344
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARP-------PTTAGPPAPAP------PAAPAAGPPRRLTRPAVASLSESR--------- 2795
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1207168553  345 vmpPQTQSPGQPAQPPMVLHQKQNRITPIQKPRGLDP 381
Cdd:PHA03247  2796 ---ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
386-554 8.55e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  386 QEREYR-LQARIA---HRIQELENLPGSLAGDLRtKANIELKALRLLNFQRQLRQEVVVCMRRDTALETalnakaykrsK 461
Cdd:COG4717     86 KEEEYAeLQEELEeleEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAELAELPERLEELEE----------R 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207168553  462 RQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSITAKMQKLTKAVATyhanTEREQKKENERIE 541
Cdd:COG4717    155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE----AQEELEELEEELE 230
                          170
                   ....*....|...
gi 1207168553  542 KERMRRLMAEDEE 554
Cdd:COG4717    231 QLENELEAAALEE 243
 
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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