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Conserved domains on  [gi|504822311|ref|WP_015009413|]
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DEAD/DEAH box helicase [Amphibacillus xylanus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12093896)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
374-1040 0e+00

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 624.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  374 PLETKLYLDLKKDALNVSVVFQYGEEKIFPNQTTQAQEQVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIY 453
Cdd:COG0553    19 ELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  454 DDLPELLEQTSVFMTDQVETLRAERDYFLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRLQNGALIKL 533
Cdd:COG0553    99 LLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  534 TDASFQAFQSLADELYFKKKDLASTSIELSPAKGLQLEHALDDSQVDysetfkQLLQTLkqpdqfdDQVPETLNAQLRDY 613
Cdd:COG0553   179 GLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR------RLREAL-------ESLPAGLKATLRPY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  614 QVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKVVSGTk 693
Cdd:COG0553   246 QLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGT- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  694 DERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEEL 773
Cdd:COG0553   325 RERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEEL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  774 WSIFQTISPGFLGPKKEFIQYPNDYI-----------RKITKPFILRRLKTDVLPDLPEKIEFEQYSELTKEQKQVYLAY 842
Cdd:COG0553   405 WSLLDFLNPGLLGSLKAFRERFARPIekgdeealerlRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  843 LERIEQQLDAVVDANQfnqeKIEILAGLTRLRQICCHPSLFLEN---YQGESGKLELLMTMIEQLRAENRRVLIFSQFSS 919
Cdd:COG0553   485 LEYLRRELEGAEGIRR----RGLILAALTRLRQICSHPALLLEEgaeLSGRSAKLEALLELLEELLAEGEKVLVFSQFTD 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  920 MLKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGER-EIFIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAG 998
Cdd:COG0553   561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEaPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAID 640
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 504822311  999 RAHRIGQTKKVEVIRLITQGTIEEKIFQLQERKRKLVDEIIQ 1040
Cdd:COG0553   641 RAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
1-525 1.39e-32

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


:

Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 133.41  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311    1 MAQFYLDTQDILKITGQRFFRRGVDLYKKGRVTKLtyNQMINSWQATVKGGNLYQVSIFFFEDDDLEAKCDCSAYQTHYt 80
Cdd:COG4715     1 MARLELTEDDIRRLAGPRIFERGREYAREGRVLDL--DVEDGRLEATVQGSEDYRVRVDLDDGGDLDSSCTCPYGGGGF- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   81 CKHIAAVLLAITKHnssttffPEQNTTEVTDPFPLRmiDMFETeqtglITKETQLKLHYQLEEkRHRVLKDTYYELQLKV 160
Cdd:COG4715    78 CKHVVAVLLALLDQ-------PEEGAPRQSEREALE--ELLER-----LSKEELVELLLELAA-EDPELRELRRALDDSG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  161 GENQLYIVKELPAFIKAIKFNEVHKITETFSYKPKDHYFDAIDLALLDMIGEAITHEELYSPDFPTVDKRSVNLPPFLIL 240
Cdd:COG4715   143 GDYLREELLELSRLAALSLTATLAALAPRSTLALRLALLRLLLLLLAPSSLDGAPPGLSLALVRELLPALAERALALLLL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  241 DFFENLISRSFEIIRDDDSIIDQLNIEQNLPKIKFPITLNEDGSFIVNFQSLFSYQFSSYYQFLNKDHEFYFLSTEQKKI 320
Cdd:COG4715   223 VPAPAGLLKLRLLLARPGALLLSLLDLLLRLDLLLGLLLLALLLLLLLLLQLLALLLLALRTLAALLLLLRLRLRLGLAA 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  321 IEQIYTILPYQKKYSYQISKAKMTHFIGYVLPQLESIGEVQYSEEAETQIKQVPLETKLYLDLKKDALNVSVVFQYGEEK 400
Cdd:COG4715   303 GLALAVLLLLLLLLLPLPLALLALSLLLRLLLALLRLALLVLLYLLLILLLLALLLLALLLLLELLLLLALLLLLAEVEL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  401 IFPNQTTQAQEQVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIYDDLPELLEQTSVFMTDQVETLRAERDY 480
Cdd:COG4715   383 ARLLEEALLIRRRLLLLLLLLLRLLDLLALLALRLLLLLLLAVLSEAEDLLLELLETLGLHRLLLLEAREELLPELAADL 462
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 504822311  481 FLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRL 525
Cdd:COG4715   463 ALLLLLEALDLLALEALALLLLLELLLLLAVTLLLLAIDELLLLA 507
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
374-1040 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 624.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  374 PLETKLYLDLKKDALNVSVVFQYGEEKIFPNQTTQAQEQVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIY 453
Cdd:COG0553    19 ELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  454 DDLPELLEQTSVFMTDQVETLRAERDYFLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRLQNGALIKL 533
Cdd:COG0553    99 LLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  534 TDASFQAFQSLADELYFKKKDLASTSIELSPAKGLQLEHALDDSQVDysetfkQLLQTLkqpdqfdDQVPETLNAQLRDY 613
Cdd:COG0553   179 GLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR------RLREAL-------ESLPAGLKATLRPY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  614 QVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKVVSGTk 693
Cdd:COG0553   246 QLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGT- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  694 DERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEEL 773
Cdd:COG0553   325 RERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEEL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  774 WSIFQTISPGFLGPKKEFIQYPNDYI-----------RKITKPFILRRLKTDVLPDLPEKIEFEQYSELTKEQKQVYLAY 842
Cdd:COG0553   405 WSLLDFLNPGLLGSLKAFRERFARPIekgdeealerlRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  843 LERIEQQLDAVVDANQfnqeKIEILAGLTRLRQICCHPSLFLEN---YQGESGKLELLMTMIEQLRAENRRVLIFSQFSS 919
Cdd:COG0553   485 LEYLRRELEGAEGIRR----RGLILAALTRLRQICSHPALLLEEgaeLSGRSAKLEALLELLEELLAEGEKVLVFSQFTD 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  920 MLKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGER-EIFIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAG 998
Cdd:COG0553   561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEaPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAID 640
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 504822311  999 RAHRIGQTKKVEVIRLITQGTIEEKIFQLQERKRKLVDEIIQ 1040
Cdd:COG0553   641 RAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
606-812 8.87e-101

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: 316.04  E-value: 8.87e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  606 LNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLS 685
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  686 VKVVSGTKDERMtIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTP 765
Cdd:cd18012    81 VLVIHGTKRKRE-KLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504822311  766 IENRLEELWSIFQTISPGFLGPKKEF-------IQYPNDY-----IRKITKPFILRRLK 812
Cdd:cd18012   160 IENHLGELWSIFDFLNPGLLGSYKRFkkrfakpIEKDGDEealeeLKKLISPFILRRLK 218
SNF2_assoc pfam08455
Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF ...
232-603 2.11e-85

Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF/SWI helicase family to the N-terminus of the SNF2 family N-terminal domain (pfam00176) and together with the Helicase conserved C-terminal domain (pfam00271). The function of the domain is not clear.


Pssm-ID: 462483  Cd Length: 370  Bit Score: 280.65  E-value: 2.11e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   232 VNLPPFLILDFFENLISRSFEIIRDDDSIIDQLNIEQNLPKIKFPITLNEDGSFIVNFQSLFsYQFSSYYQFLNKDHEFY 311
Cdd:pfam08455    1 LVLPPSLLDEFLELLKGRKFYLELDEGEELKEVKIVEENPPLSFSLKKEKDDGIILTLNKDP-ILLGEDYLYFLYDGTIY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   312 FLSTEQKKIIEQIYTILPYQKKYSYQISKAKMTHFIGYVLPQLESIGEVQYSEEAETQIKQVPLETKLYLDLKKDALNVS 391
Cdd:pfam08455   80 RLSKEQCKLLSPLLKLLNLLGTKEITISKEDLPKFLSEVLPKLKKIGEVEIPEELLEKYVPEPLKAKFYLDRDDDRITAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   392 VVFQYGEEKIFPNQTTqaqeqVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIYDDLPELLEQTSVFMTDQV 471
Cdd:pfam08455  160 VKFQYGDIEFNPLEDL-----ILVRDVEKEAKILNLLEQYGFKVDDGKFYLDDEEKIYDFLTEGLPKLQELGEVYYSDAF 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   472 ETLRAERDYFLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRLQNGALIKLTDASFQAFQSLADELYFK 551
Cdd:pfam08455  235 KNLKVKPSPSVSVGVSVDEEGNLLEISFDIDGIDEEELANILQALREKKKYYRLKDGSFLDLEEEELKELSELLDELGLS 314
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 504822311   552 KKDLASTSIELSPAKGLQLEHALDDS----QVDYSETFKQLLQTLKQPDQFDDQVP 603
Cdd:pfam08455  315 KKDLENGTIKLPKYRALYLDELLEENeligSIKRDKEFKQLVEDLKNPEDSDFEVP 370
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
603-1060 9.72e-83

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 290.93  E-value: 9.72e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  603 PETLNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFA 681
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGItGPHMVVAPKSTLGNWMNEIRRFC 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  682 PTLSVKVVSGTKDERMTIIKDNHEP---DVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQR 758
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQREELLVAgkfDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  759 FALSGTPIENRLEELWSIFQTISPGFLGPKKEF-----IQYPND------YIRKITKPFILRRLKTDVLPDLPEKIEFEQ 827
Cdd:PLN03142  323 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFdewfqISGENDqqevvqQLHKVLRPFLLRRLKSDVEKGLPPKKETIL 402
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  828 YSELTKEQKQVYLAYLERieqQLDAVvdanQFNQEKIEILAGLTRLRQICCHPSLF---------------LENyqgeSG 892
Cdd:PLN03142  403 KVGMSQMQKQYYKALLQK---DLDVV----NAGGERKRLLNIAMQLRKCCNHPYLFqgaepgppyttgehlVEN----SG 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  893 KLELLMTMIEQLRAENRRVLIFSQFSSMLKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFN--NGEREIFIISLKAGG 970
Cdd:PLN03142  472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpGSEKFVFLLSTRAGG 551
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  971 TGLNLTGADTVILFDLWWNPAVEAQAAGRAHRIGQTKKVEVIRLITQGTIEEKIFQLQERKRKLVDEIIQPGE-TLLSSL 1049
Cdd:PLN03142  552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRlAEQKTV 631
                         490
                  ....*....|.
gi 504822311 1050 NEKELRELLTF 1060
Cdd:PLN03142  632 NKDELLQMVRY 642
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
1-525 1.39e-32

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 133.41  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311    1 MAQFYLDTQDILKITGQRFFRRGVDLYKKGRVTKLtyNQMINSWQATVKGGNLYQVSIFFFEDDDLEAKCDCSAYQTHYt 80
Cdd:COG4715     1 MARLELTEDDIRRLAGPRIFERGREYAREGRVLDL--DVEDGRLEATVQGSEDYRVRVDLDDGGDLDSSCTCPYGGGGF- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   81 CKHIAAVLLAITKHnssttffPEQNTTEVTDPFPLRmiDMFETeqtglITKETQLKLHYQLEEkRHRVLKDTYYELQLKV 160
Cdd:COG4715    78 CKHVVAVLLALLDQ-------PEEGAPRQSEREALE--ELLER-----LSKEELVELLLELAA-EDPELRELRRALDDSG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  161 GENQLYIVKELPAFIKAIKFNEVHKITETFSYKPKDHYFDAIDLALLDMIGEAITHEELYSPDFPTVDKRSVNLPPFLIL 240
Cdd:COG4715   143 GDYLREELLELSRLAALSLTATLAALAPRSTLALRLALLRLLLLLLAPSSLDGAPPGLSLALVRELLPALAERALALLLL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  241 DFFENLISRSFEIIRDDDSIIDQLNIEQNLPKIKFPITLNEDGSFIVNFQSLFSYQFSSYYQFLNKDHEFYFLSTEQKKI 320
Cdd:COG4715   223 VPAPAGLLKLRLLLARPGALLLSLLDLLLRLDLLLGLLLLALLLLLLLLLQLLALLLLALRTLAALLLLLRLRLRLGLAA 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  321 IEQIYTILPYQKKYSYQISKAKMTHFIGYVLPQLESIGEVQYSEEAETQIKQVPLETKLYLDLKKDALNVSVVFQYGEEK 400
Cdd:COG4715   303 GLALAVLLLLLLLLLPLPLALLALSLLLRLLLALLRLALLVLLYLLLILLLLALLLLALLLLLELLLLLALLLLLAEVEL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  401 IFPNQTTQAQEQVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIYDDLPELLEQTSVFMTDQVETLRAERDY 480
Cdd:COG4715   383 ARLLEEALLIRRRLLLLLLLLLRLLDLLALLALRLLLLLLLAVLSEAEDLLLELLETLGLHRLLLLEAREELLPELAADL 462
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 504822311  481 FLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRL 525
Cdd:COG4715   463 ALLLLLEALDLLALEALALLLLLELLLLLAVTLLLLAIDELLLLA 507
HELICc smart00490
helicase superfamily c-terminal domain;
922-1004 1.52e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 1.52e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311    922 KIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGEReIFIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAGRAH 1001
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI-KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                    ...
gi 504822311   1002 RIG 1004
Cdd:smart00490   80 RAG 82
DpdE NF041062
protein DpdE;
626-771 1.70e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 55.75  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  626 RYqlggILADEMGLGKTIQAiSFILSEKTTEKigPS---IVIAPASLIYNWKKEF-EKFA----PTLSVKVVSgtkderm 697
Cdd:NF041062  172 RY----LLADEVGLGKTIEA-GLVIRQHLLDN--PDarvLVLVPDALVRQWRRELrDKFFlddfPGARVRVLS------- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  698 tiikdnHE-PDVWITsypllrqdvklyKHMYFDVMILDEAQaiknHLTQTAKATRQIQaKQRFA--------------LS 762
Cdd:NF041062  238 ------HEePERWEP------------LLDAPDLLVVDEAH----QLARLAWSGDPPE-RARYRelaalahaaprlllLS 294

                  ....*....
gi 504822311  763 GTPIENRLE 771
Cdd:NF041062  295 ATPVLGNEE 303
SWIM pfam04434
SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is ...
54-91 2.15e-05

SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is predicted to be organized into two N-terminal beta-strands and a C-terminal alpha helix, thus possibly adopting a fold similar to that of the C2H2 zinc finger (pfam00096). SWIM is thought to be a versatile domain that can interact with DNA or proteins in different contexts.


Pssm-ID: 309540  Cd Length: 38  Bit Score: 42.41  E-value: 2.15e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 504822311    54 YQVSIFffEDDDLEAKCDCSAYQ-THYTCKHIAAVLLAI 91
Cdd:pfam04434    1 YRVQLD--LDGLEKASCSCPDFQlNGIPCKHALAVLLAL 37
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
374-1040 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 624.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  374 PLETKLYLDLKKDALNVSVVFQYGEEKIFPNQTTQAQEQVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIY 453
Cdd:COG0553    19 ELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  454 DDLPELLEQTSVFMTDQVETLRAERDYFLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRLQNGALIKL 533
Cdd:COG0553    99 LLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  534 TDASFQAFQSLADELYFKKKDLASTSIELSPAKGLQLEHALDDSQVDysetfkQLLQTLkqpdqfdDQVPETLNAQLRDY 613
Cdd:COG0553   179 GLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR------RLREAL-------ESLPAGLKATLRPY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  614 QVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKVVSGTk 693
Cdd:COG0553   246 QLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGT- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  694 DERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEEL 773
Cdd:COG0553   325 RERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEEL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  774 WSIFQTISPGFLGPKKEFIQYPNDYI-----------RKITKPFILRRLKTDVLPDLPEKIEFEQYSELTKEQKQVYLAY 842
Cdd:COG0553   405 WSLLDFLNPGLLGSLKAFRERFARPIekgdeealerlRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  843 LERIEQQLDAVVDANQfnqeKIEILAGLTRLRQICCHPSLFLEN---YQGESGKLELLMTMIEQLRAENRRVLIFSQFSS 919
Cdd:COG0553   485 LEYLRRELEGAEGIRR----RGLILAALTRLRQICSHPALLLEEgaeLSGRSAKLEALLELLEELLAEGEKVLVFSQFTD 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  920 MLKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGER-EIFIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAG 998
Cdd:COG0553   561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEaPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAID 640
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 504822311  999 RAHRIGQTKKVEVIRLITQGTIEEKIFQLQERKRKLVDEIIQ 1040
Cdd:COG0553   641 RAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
606-812 8.87e-101

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: 316.04  E-value: 8.87e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  606 LNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLS 685
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  686 VKVVSGTKDERMtIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTP 765
Cdd:cd18012    81 VLVIHGTKRKRE-KLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504822311  766 IENRLEELWSIFQTISPGFLGPKKEF-------IQYPNDY-----IRKITKPFILRRLK 812
Cdd:cd18012   160 IENHLGELWSIFDFLNPGLLGSYKRFkkrfakpIEKDGDEealeeLKKLISPFILRRLK 218
SNF2_assoc pfam08455
Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF ...
232-603 2.11e-85

Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF/SWI helicase family to the N-terminus of the SNF2 family N-terminal domain (pfam00176) and together with the Helicase conserved C-terminal domain (pfam00271). The function of the domain is not clear.


Pssm-ID: 462483  Cd Length: 370  Bit Score: 280.65  E-value: 2.11e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   232 VNLPPFLILDFFENLISRSFEIIRDDDSIIDQLNIEQNLPKIKFPITLNEDGSFIVNFQSLFsYQFSSYYQFLNKDHEFY 311
Cdd:pfam08455    1 LVLPPSLLDEFLELLKGRKFYLELDEGEELKEVKIVEENPPLSFSLKKEKDDGIILTLNKDP-ILLGEDYLYFLYDGTIY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   312 FLSTEQKKIIEQIYTILPYQKKYSYQISKAKMTHFIGYVLPQLESIGEVQYSEEAETQIKQVPLETKLYLDLKKDALNVS 391
Cdd:pfam08455   80 RLSKEQCKLLSPLLKLLNLLGTKEITISKEDLPKFLSEVLPKLKKIGEVEIPEELLEKYVPEPLKAKFYLDRDDDRITAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   392 VVFQYGEEKIFPNQTTqaqeqVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIYDDLPELLEQTSVFMTDQV 471
Cdd:pfam08455  160 VKFQYGDIEFNPLEDL-----ILVRDVEKEAKILNLLEQYGFKVDDGKFYLDDEEKIYDFLTEGLPKLQELGEVYYSDAF 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   472 ETLRAERDYFLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRLQNGALIKLTDASFQAFQSLADELYFK 551
Cdd:pfam08455  235 KNLKVKPSPSVSVGVSVDEEGNLLEISFDIDGIDEEELANILQALREKKKYYRLKDGSFLDLEEEELKELSELLDELGLS 314
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 504822311   552 KKDLASTSIELSPAKGLQLEHALDDS----QVDYSETFKQLLQTLKQPDQFDDQVP 603
Cdd:pfam08455  315 KKDLENGTIKLPKYRALYLDELLEENeligSIKRDKEFKQLVEDLKNPEDSDFEVP 370
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
603-1060 9.72e-83

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 290.93  E-value: 9.72e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  603 PETLNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFA 681
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGItGPHMVVAPKSTLGNWMNEIRRFC 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  682 PTLSVKVVSGTKDERMTIIKDNHEP---DVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQR 758
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQREELLVAgkfDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  759 FALSGTPIENRLEELWSIFQTISPGFLGPKKEF-----IQYPND------YIRKITKPFILRRLKTDVLPDLPEKIEFEQ 827
Cdd:PLN03142  323 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFdewfqISGENDqqevvqQLHKVLRPFLLRRLKSDVEKGLPPKKETIL 402
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  828 YSELTKEQKQVYLAYLERieqQLDAVvdanQFNQEKIEILAGLTRLRQICCHPSLF---------------LENyqgeSG 892
Cdd:PLN03142  403 KVGMSQMQKQYYKALLQK---DLDVV----NAGGERKRLLNIAMQLRKCCNHPYLFqgaepgppyttgehlVEN----SG 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  893 KLELLMTMIEQLRAENRRVLIFSQFSSMLKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFN--NGEREIFIISLKAGG 970
Cdd:PLN03142  472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpGSEKFVFLLSTRAGG 551
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  971 TGLNLTGADTVILFDLWWNPAVEAQAAGRAHRIGQTKKVEVIRLITQGTIEEKIFQLQERKRKLVDEIIQPGE-TLLSSL 1049
Cdd:PLN03142  552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRlAEQKTV 631
                         490
                  ....*....|.
gi 504822311 1050 NEKELRELLTF 1060
Cdd:PLN03142  632 NKDELLQMVRY 642
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
613-883 3.12e-63

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: 216.40  E-value: 3.12e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   613 YQVTGFKWFkaLARYQ---LGGILADEMGLGKTIQAISFI--LSEKTTEKIGPSIVIAPASLIYNWKKEFEKFA--PTLS 685
Cdd:pfam00176    1 YQIEGVNWM--LSLENnlgRGGILADEMGLGKTLQTISLLlyLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   686 VKVVSGTKDERMTIIKDNHEP---DVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALS 762
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLadfDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   763 GTPIENRLEELWSIFQTISPGFLGPKKEF-------IQYPNDY-----IRKITKPFILRRLKTDVLPDLPEKIEFEQYSE 830
Cdd:pfam00176  159 GTPLQNNLEELWALLNFLRPGPFGSLSTFrnwfdrpIERGGGKkgvsrLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCR 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 504822311   831 LTKEQKQVYLAYLERIEqqLDAVVDANQFNQEKIEILAGLTRLRQICCHPSLF 883
Cdd:pfam00176  239 LSKLQRKLYQTFLLKKD--LNAIKTGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
610-810 1.36e-61

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: 207.80  E-value: 1.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEK-IGPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKeRGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERMTIIKDNHEP--DVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPI 766
Cdd:cd17919    81 YHGSQRERAQIRAKEKLDkfDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 504822311  767 ENRLEELWSIFQtispgFLGPkkefiqypndyirkitkPFILRR 810
Cdd:cd17919   161 QNNLEELWALLD-----FLDP-----------------PFLLRR 182
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
891-1015 9.47e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.92  E-value: 9.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  891 SGKLELLMTMIEQLRAENRRVLIFSQFSSMLKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGERE-IFIISLKAG 969
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 504822311  970 GTGLNLTGADTVILFDLWWNPAVEAQAAGRAHRIGQTKKVEVIRLI 1015
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
610-810 6.60e-53

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: 184.86  E-value: 6.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFI------LSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPT 683
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILasdhhkRANSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  684 LSVKVV--SGTKDERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFAL 761
Cdd:cd17999    81 AFLKPLayVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504822311  762 SGTPIENRLEELWSIFQTISPGFLGPKKEFIQypnDYIRKITK--------------------------PFILRR 810
Cdd:cd17999   161 SGTPIQNNVLELWSLFDFLMPGYLGTEKQFQR---RFLKPILAsrdskasakeqeagalalealhkqvlPFLLRR 232
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
607-812 2.44e-49

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: 174.43  E-value: 2.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  607 NAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFAPTLS 685
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNInGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  686 VKVVSGTKDERMTIIKDNHEP---DVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALS 762
Cdd:cd17997    81 VVVLIGDKEERADIIRDVLLPgkfDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504822311  763 GTPIENRLEELWSIFQTISPGFLGPKKEFIQYPN------------DYIRKITKPFILRRLK 812
Cdd:cd17997   161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNvnncdddnqevvQRLHKVLRPFLLRRIK 222
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
610-810 6.62e-47

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


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 167.93  E-value: 6.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKVV 689
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  690 SGT-KDERMTI---IKDNHepDVWITSYPLLR---QDVKLYKHMYF--DVMILDEAQAIKNHLTQTAKATRQIQAKQRFA 760
Cdd:cd18001    81 HGTsKKERERNlerIQRGG--GVLLTTYGMVLsntEQLSADDHDEFkwDYVILDEGHKIKNSKTKSAKSLREIPAKNRII 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504822311  761 LSGTPIENRLEELWSIFQTISPG-FLGPKKEFIQYPNDYI-----------------------RKITKPFILRR 810
Cdd:cd18001   159 LTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPItrgrdkdatqgekalgsevaenlRQIIKPYFLRR 232
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
610-810 9.77e-46

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: 164.06  E-value: 9.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNwGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERMTIIKDNHEPDVW---ITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTP 765
Cdd:cd18003    81 YYGSAKERKLKRQGWMKPNSFhvcITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504822311  766 IENRLEELWSIFQTISPGFLGPKKEFIQYPNDYIR------------------KITKPFILRR 810
Cdd:cd18003   161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsqeeneelvrrlhKVLRPFLLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
607-812 6.64e-44

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: 159.47  E-value: 6.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  607 NAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSV 686
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  687 KVVSGTKDERMTIIKDNHEPD-------VWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRF 759
Cdd:cd18009    81 LLYHGTKEERERLRKKIMKREgtlqdfpVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504822311  760 ALSGTPIENRLEELWSIFQTISP-------------GFLGPKK----------EFIQYPNDYIRKITKPFILRRLK 812
Cdd:cd18009   161 LLTGTPLQNNLSELWSLLNFLLPdvfddlssfeswfDFSSLSDnaadisnlseEREQNIVHMLHAILKPFLLRRLK 236
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
610-810 3.02e-43

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: 155.94  E-value: 3.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEK-IGPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLgLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 ----VSGTKDER---------MTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQA 755
Cdd:cd18000    81 lhssGSGTGSEEklgsierksQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504822311  756 KQRFALSGTPIENRLEELWSIFqtispgflgpkkEFIqYPndyirkitkPFILRR 810
Cdd:cd18000   161 PHRLILSGTPIQNNLKELWSLF------------DFV-FP---------PYLLRR 193
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
610-810 2.33e-42

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


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 155.14  E-value: 2.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWfkALARyqlGGILADEMGLGKTIQAISFILS------------------EKTTEKIGPSIVIAPASLIY 671
Cdd:cd18008     1 LLPYQKQGLAW--MLPR---GGILADEMGLGKTIQALALILAtrpqdpkipeeleenssdPKKLYLSKTTLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  672 NWKKEFEKF--APTLSVKVVSGtkDERMTIIKDNHEPDVWITSYPLLRQDVK-----------------LYKHMYFDVmI 732
Cdd:cd18008    76 QWKDEIEKHtkPGSLKVYVYHG--SKRIKSIEELSDYDIVITTYGTLASEFPknkkgggrdskekeaspLHRIRWYRV-I 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  733 LDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQY-----------PNDYIRK 801
Cdd:cd18008   153 LDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDiskpfskndrkALERLQA 232

                  ....*....
gi 504822311  802 ITKPFILRR 810
Cdd:cd18008   233 LLKPILLRR 241
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
610-810 3.75e-42

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: 152.54  E-value: 3.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKVV 689
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  690 SGTKDERMTI---IKDNHEP-DVWITSYPLL---RQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALS 762
Cdd:cd17998    81 YGSQEERKHLrydILKGLEDfDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 504822311  763 GTPIENRLEELWSIFQTISPgflgpkkefiqypndyirkitKPFILRR 810
Cdd:cd17998   161 GTPLQNNLLELMSLLNFIMP---------------------KPFILRR 187
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
597-822 8.22e-42

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: 153.67  E-value: 8.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  597 QFDDQVPETLNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKK 675
Cdd:cd18064     3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIpGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  676 EFEKFAPTLSVKVVSGTKDERMTIIKDNHEP---DVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQ 752
Cdd:cd18064    83 EFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPgewDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  753 IQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPN-----------DYIRKITKPFILRRLKTDVLPDLPE 821
Cdd:cd18064   163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDtnnclgdqklvERLHMVLRPFLLRRIKADVEKSLPP 242

                  .
gi 504822311  822 K 822
Cdd:cd18064   243 K 243
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
610-791 4.70e-41

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: 151.38  E-value: 4.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISF---ILSEKTTEKI------------------GPSIVIAPAS 668
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFlaaVLGKTGTRRDrennrprfkkkppassakKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  669 LIYNWKKEFEKFAPTLSVKVVSGTKDERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAK 748
Cdd:cd18005    81 VLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 504822311  749 ATRQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEF 791
Cdd:cd18005   161 AMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQF 203
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
610-810 6.95e-41

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: 150.35  E-value: 6.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIwGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERMTIIK---------DNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRF 759
Cdd:cd18002    81 YWGNPKDRKVLRKfwdrknlytRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504822311  760 ALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPNDYIRK------------------ITKPFILRR 810
Cdd:cd18002   161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEShaenktglnehqlkrlhmILKPFMLRR 229
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
607-812 4.85e-39

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: 145.20  E-value: 4.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  607 NAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFI--LSEKTTEKiGPSIVIAPASLIYNWKKEFEKFAPTL 684
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLItyLMEKKKNN-GPYLVIVPLSTLSNWVSEFEKWAPSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  685 SVKVVSGTKDERMTIIKD--NHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNH---LTQTAKatRQIQAKQRF 759
Cdd:cd17996    80 SKIVYKGTPDVRKKLQSQirAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAqskLTQTLN--TYYHARYRL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504822311  760 ALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPND--------------------YIR---KITKPFILRRLK 812
Cdd:cd17996   158 LLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfantgeqvkielneeetllIIRrlhKVLRPFLLRRLK 233
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
610-812 6.48e-38

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: 142.08  E-value: 6.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIpGPHMVLVPKSTLHNWMNEFKRWVPSLRAVC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERMTIIKDNHEP---DVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTP 765
Cdd:cd18065    96 LIGDKDARAAFIRDVMMPgewDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 504822311  766 IENRLEELWSIFQTISPGFLGPKKEFIQYPN-----------DYIRKITKPFILRRLK 812
Cdd:cd18065   176 LQNNLHELWALLNFLLPDVFNSADDFDSWFDtknclgdqklvERLHAVLKPFLLRRIK 233
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
610-810 2.79e-37

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: 140.50  E-value: 2.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKW-FKALARYQLGG----ILADEMGLGKTIQAISFI--------LSEKTTEKIgpsIVIAPASLIYNWKKE 676
Cdd:cd18004     1 LRPHQREGVQFlYDCLTGRRGYGgggaILADEMGLGKTLQAIALVwtllkqgpYGKPTAKKA---LIVCPSSLVGNWKAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  677 FEKFAPTLSVKVV---SGTKDERMTIIKDNHEP--DVWITSYPLLRQDVKLYKH-MYFDVMILDEAQAIKNHLTQTAKAT 750
Cdd:cd18004    78 FDKWLGLRRIKVVtadGNAKDVKASLDFFSSAStyPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  751 RQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEF-------IQYPND----------------YIRKITKPFI 807
Cdd:cd18004   158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFrkvfeepILRSRDpdaseedkelgaersqELSELTSRFI 237

                  ...
gi 504822311  808 LRR 810
Cdd:cd18004   238 LRR 240
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
610-810 6.04e-37

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: 138.72  E-value: 6.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLlGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERMTI---IKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTP 765
Cdd:cd18006    81 YMGDKEKRLDLqqdIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 504822311  766 IENRLEELWSIFQTISPGFLGPKK--EFIQYPNDY---------IRKITKPFILRR 810
Cdd:cd18006   161 IQNSLQELYALLSFIEPNVFPKDKldDFIKAYSETddesetveeLHLLLQPFLLRR 216
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
630-802 5.62e-35

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: 133.57  E-value: 5.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  630 GGILADEMGLGKTIQAISFILS-------EKTTekigpsIVIAPASLIYNWKKEFEKFAP-------TLSVKVVSGTKDE 695
Cdd:cd18007    28 GCILAHTMGLGKTLQVITFLHTylaaaprRSRP------LVLCPASTLYNWEDEFKKWLPpdlrpllVLVSLSASKRADA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  696 RMTIIKDNH-EPDVWITSYPLLR------QDVKLYKHMYF--------DVMILDEAQAIKNHLTQTAKATRQIQAKQRFA 760
Cdd:cd18007   102 RLRKINKWHkEGGVLLIGYELFRnlasnaTTDPRLKQEFIaalldpgpDLLVLDEGHRLKNEKSQLSKALSKVKTKRRIL 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 504822311  761 LSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYpndYIRKI 802
Cdd:cd18007   182 LTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKK---FVKPI 220
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
609-810 2.84e-34

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: 130.94  E-value: 2.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  609 QLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILS-EKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVK 687
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYlFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  688 VVSGTKDERMTI------------IKDNhepdVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQA 755
Cdd:cd17993    81 VYLGDIKSRDTIreyefyfsqtkkLKFN----VLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKT 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504822311  756 KQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPN----DYIRKITK---PFILRR 810
Cdd:cd17993   157 NNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDeeqeKGIADLHKelePFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
610-810 6.51e-34

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: 130.06  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFApTLSVKV 688
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIrGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERMTI--------------IKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQ 754
Cdd:cd17995    80 YHGSGESRQIIqqyemyfkdaqgrkKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504822311  755 AKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQypnDY-----------IRKITKPFILRR 810
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLE---EFgdlktaeqvekLQALLKPYMLRR 223
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
1-525 1.39e-32

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 133.41  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311    1 MAQFYLDTQDILKITGQRFFRRGVDLYKKGRVTKLtyNQMINSWQATVKGGNLYQVSIFFFEDDDLEAKCDCSAYQTHYt 80
Cdd:COG4715     1 MARLELTEDDIRRLAGPRIFERGREYAREGRVLDL--DVEDGRLEATVQGSEDYRVRVDLDDGGDLDSSCTCPYGGGGF- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   81 CKHIAAVLLAITKHnssttffPEQNTTEVTDPFPLRmiDMFETeqtglITKETQLKLHYQLEEkRHRVLKDTYYELQLKV 160
Cdd:COG4715    78 CKHVVAVLLALLDQ-------PEEGAPRQSEREALE--ELLER-----LSKEELVELLLELAA-EDPELRELRRALDDSG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  161 GENQLYIVKELPAFIKAIKFNEVHKITETFSYKPKDHYFDAIDLALLDMIGEAITHEELYSPDFPTVDKRSVNLPPFLIL 240
Cdd:COG4715   143 GDYLREELLELSRLAALSLTATLAALAPRSTLALRLALLRLLLLLLAPSSLDGAPPGLSLALVRELLPALAERALALLLL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  241 DFFENLISRSFEIIRDDDSIIDQLNIEQNLPKIKFPITLNEDGSFIVNFQSLFSYQFSSYYQFLNKDHEFYFLSTEQKKI 320
Cdd:COG4715   223 VPAPAGLLKLRLLLARPGALLLSLLDLLLRLDLLLGLLLLALLLLLLLLLQLLALLLLALRTLAALLLLLRLRLRLGLAA 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  321 IEQIYTILPYQKKYSYQISKAKMTHFIGYVLPQLESIGEVQYSEEAETQIKQVPLETKLYLDLKKDALNVSVVFQYGEEK 400
Cdd:COG4715   303 GLALAVLLLLLLLLLPLPLALLALSLLLRLLLALLRLALLVLLYLLLILLLLALLLLALLLLLELLLLLALLLLLAEVEL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  401 IFPNQTTQAQEQVLVRDFQAEQALLTRLKNSGFRLLNQSYWLFSEEKMYQFIYDDLPELLEQTSVFMTDQVETLRAERDY 480
Cdd:COG4715   383 ARLLEEALLIRRRLLLLLLLLLRLLDLLALLALRLLLLLLLAVLSEAEDLLLELLETLGLHRLLLLEAREELLPELAADL 462
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 504822311  481 FLDTRVEVNALTGMLDVQFNIDGITKQDVQNVLQALVEKKSYHRL 525
Cdd:COG4715   463 ALLLLLEALDLLALEALALLLLLELLLLLAVTLLLLAIDELLLLA 507
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
610-794 8.29e-32

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: 123.85  E-value: 8.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWfkALARyqlGG--ILADEMGLGKTIQAISFILSEKtteKIGPSIVIAPASLIYNWKKEFEKFAPTLSVK 687
Cdd:cd18010     1 LLPFQREGVCF--ALRR---GGrvLIADEMGLGKTVQAIAIAAYYR---EEWPLLIVCPSSLRLTWADEIERWLPSLPPD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  688 ---VVSGTKDERMTiikdnHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQI--QAKQRFALS 762
Cdd:cd18010    73 diqVIVKSKDGLRD-----GDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILLS 147
                         170       180       190
                  ....*....|....*....|....*....|..
gi 504822311  763 GTPIENRLEELWSIFQTISPGFLGPKKEFIQY 794
Cdd:cd18010   148 GTPALSRPIELFTQLDALDPKLFGRFHDFGRR 179
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
596-812 7.71e-30

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: 119.38  E-value: 7.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  596 DQFDDQVPETLNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWK 674
Cdd:cd18062    10 EKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRInGPFLIIVPLSTLSNWV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  675 KEFEKFAPTLSVKVVSGTKDERMTIIKD--NHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNH---LTQTAKA 749
Cdd:cd18062    90 YEFDKWAPSVVKVSYKGSPAARRAFVPQlrSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHhckLTQVLNT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  750 trQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPN---------------------DYIRKITKPFIL 808
Cdd:cd18062   170 --HYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvdlneeetiliiRRLHKVLRPFLL 247

                  ....
gi 504822311  809 RRLK 812
Cdd:cd18062   248 RRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
596-812 1.13e-29

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: 119.01  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  596 DQFDDQVPETLNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWK 674
Cdd:cd18063    10 ERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLnGPYLIIVPLSTLSNWT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  675 KEFEKFAPTLSVKVVSGTKDERMTIIKD--NHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNH---LTQTAKA 749
Cdd:cd18063    90 YEFDKWAPSVVKISYKGTPAMRRSLVPQlrSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHhckLTQVLNT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  750 trQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPN---------------------DYIRKITKPFIL 808
Cdd:cd18063   170 --HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervdlneeetiliiRRLHKVLRPFLL 247

                  ....
gi 504822311  809 RRLK 812
Cdd:cd18063   248 RRLK 251
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
593-810 1.25e-29

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: 118.18  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  593 KQPDQFDDQvpetlNAQLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIY 671
Cdd:cd18054     9 KQPSYIGGE-----NLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLyGPFLLVVPLSTLT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  672 NWKKEFEKFAPTLSVKVVSGTKDERMTI------------IKDNhepdVWITSYPLLRQDVKLYKHMYFDVMILDEAQAI 739
Cdd:cd18054    84 SWQREFEIWAPEINVVVYIGDLMSRNTIreyewihsqtkrLKFN----ALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504822311  740 KNHLTQTAKATRQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQ-----YPNDY--IRKITKPFILRR 810
Cdd:cd18054   160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEdhgkgRENGYqsLHKVLEPFLLRR 237
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
630-810 3.64e-28

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: 114.11  E-value: 3.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  630 GGILADEMGLGKTIQAISFILSEKTTEKI-----------------------GPSIVIAPASLIYNWKKEFEKFAPTLSV 686
Cdd:cd18072    22 GGILADDMGLGKTLTMIALILAQKNTQNRkeeekekalteweskkdstlvpsAGTLVVCPASLVHQWKNEVESRVASNKL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  687 KVVSGTKDERMTIIKDNHEPDVWITSYPLLRQDVKLYKH---------MYFDVMILDEAQAIKNHLTQTAKATRQIQAKQ 757
Cdd:cd18072   102 RVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEesrssplfrIAWARIILDEAHNIKNPKVQASIAVCKLRAHA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504822311  758 RFALSGTPIENRLEELWSIFQtispgFL--GPKKEFIQYPNDYIRK----------ITKPFILRR 810
Cdd:cd18072   182 RWALTGTPIQNNLLDMYSLLK-----FLrcSPFDDLKVWKKQVDNKsrkggerlniLTKSLLLRR 241
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
892-1004 4.82e-28

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 109.22  E-value: 4.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   892 GKLELLMTMIEqlRAENRRVLIFSQFSSMLKIiEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGEReIFIISLKAGGT 971
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKI-DVLVATDVAER 76
                           90       100       110
                   ....*....|....*....|....*....|...
gi 504822311   972 GLNLTGADTVILFDLWWNPAVEAQAAGRAHRIG 1004
Cdd:pfam00271   77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
630-833 2.81e-27

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: 111.48  E-value: 2.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  630 GGILADEMGLGKTIQAISFILsekTTEKIGP---------SIVIAPASLIYNWKKEFEKFAPTLSVKVVSGTKDERMTII 700
Cdd:cd18066    26 GAILADEMGLGKTLQCISLIW---TLLRQGPyggkpvikrALIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQDHKVEEF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  701 KDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEELWSIFQTI 780
Cdd:cd18066   103 IASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFV 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504822311  781 SPGFLGPKKEFiqypndyiRKITKPFILRRLKTDVLPDlPEKIEFEQYSELTK 833
Cdd:cd18066   183 NPGILGSLSTY--------RKVYEEPIVRSREPTATPE-EKKLGEARAAELTR 226
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
610-782 1.72e-25

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: 104.83  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILS-EKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVkv 688
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSlYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 vsgtkderMTIIKDNhepdVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIEN 768
Cdd:cd17994    79 --------VTYVGDH----VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQN 146
                         170
                  ....*....|....
gi 504822311  769 RLEELWSIFQTISP 782
Cdd:cd17994   147 NLEELFHLLNFLTP 160
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
629-777 2.11e-25

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: 106.01  E-value: 2.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  629 LGGILADEMGLGKTIQAISFILSEKTtekigpsIVIAPASLIYNWKKEFEKFAPTLSVKVVSGTKDERMTIIKDNHEPDV 708
Cdd:cd18071    49 RGGILADDMGLGKTLTTISLILANFT-------LIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLSKYDI 121
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504822311  709 WITSYPLLRQDVKL-----YKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEELWSIF 777
Cdd:cd18071   122 VLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLL 195
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
610-810 7.11e-25

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: 103.98  E-value: 7.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFApTLSVKVV 689
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  690 SGT--------------KDERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQA 755
Cdd:cd18060    80 HGSlasrqmiqqyemycKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504822311  756 KQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPNDY--------IRKITKPFILRR 810
Cdd:cd18060   160 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLkteeqvqkLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
610-810 1.40e-24

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: 103.19  E-value: 1.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFApTLSVKVV 689
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  690 SGTKDERMTI--------------IKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQA 755
Cdd:cd18059    80 HGSQASRRTIqlyemyfkdpqgrvIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504822311  756 KQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPNDY--------IRKITKPFILRR 810
Cdd:cd18059   160 EHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLkteeqvqkLQAILKPMMLRR 222
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
610-792 2.04e-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: 102.97  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWF-----KALARYQ----LGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKF 680
Cdd:cd18069     1 LKPHQIGGIRFLydniiESLERYKgssgFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  681 APTLS---------VKV-----VSGTKDERMTIIKD-NHEPDVWITSYPLLRQDVKLykhmyfDVMILDEAQAIKNHLTQ 745
Cdd:cd18069    81 LPPPEalpnvrprpFKVfilndEHKTTAARAKVIEDwVKDGGVLLMGYEMFRLRPGP------DVVICDEGHRIKNCHAS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 504822311  746 TAKATRQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFI 792
Cdd:cd18069   155 TSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFS 201
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
610-804 4.00e-24

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: 102.66  E-value: 4.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTG--FKW---FKALARYQ----LGGILADEMGLGKTIQAISF---ILSEKTTEKIGPSIVIAPASLIYNWKKEF 677
Cdd:cd18068     1 LKPHQVDGvqFMWdccCESLKKTKkspgSGCILAHCMGLGKTLQVVTFlhtVLLCEKLENFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  678 EKF------APTLSVKVVSGTKDERMTIIKDNH---EPDVWITSYPLLR-----QDVKLYKHMYFDVM-----------I 732
Cdd:cd18068    81 EKWqeglkdEEKIEVNELATYKRPQERSYKLQRwqeEGGVMIIGYDMYRilaqeRNVKSREKLKEIFNkalvdpgpdfvV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504822311  733 LDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIqypNDYIRKITK 804
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFR---NRFVNPIQN 229
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
610-810 6.62e-24

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: 101.27  E-value: 6.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFiLSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFApTLSVKV 688
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITF-LSEIFLMGIrGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGT--------------KDERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQ 754
Cdd:cd18058    79 YHGSqisrqmiqqyemyyRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504822311  755 AKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPNDY--------IRKITKPFILRR 810
Cdd:cd18058   159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLkteeqvkkLQSILKPMMLRR 222
HELICc smart00490
helicase superfamily c-terminal domain;
922-1004 1.52e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 1.52e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311    922 KIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGEReIFIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAGRAH 1001
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI-KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                    ...
gi 504822311   1002 RIG 1004
Cdd:smart00490   80 RAG 82
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
610-791 3.29e-23

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: 99.85  E-value: 3.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKW-FKALARYQLGG----ILADEMGLGKTIQAISFIL-----SEKTTEKIGPSIVIAPASLIYNWKKEFEK 679
Cdd:cd18067     1 LRPHQREGVKFlYRCVTGRRIRGshgcIMADEMGLGKTLQCITLMWtllrqSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  680 F--APTLSVKVVSGTKDE--RMTIIKDNHE-----PDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKAT 750
Cdd:cd18067    81 WlgGRLQPLAIDGGSKKEidRKLVQWASQQgrrvsTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 504822311  751 RQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEF 791
Cdd:cd18067   161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEF 201
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
610-810 4.08e-23

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: 99.37  E-value: 4.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILS-EKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSlYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERmTIIKDNH-----------------------EPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQ 745
Cdd:cd18056    81 YVGDKDSR-AIIRENEfsfednairggkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504822311  746 TAKATRQIQAKQRFALSGTPIENRLEELWSIFQTISP-------GFLgpkKEFIQYPN-DYIRKITK---PFILRR 810
Cdd:cd18056   160 FFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPerfhnleGFL---EEFADIAKeDQIKKLHDmlgPHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
610-810 4.94e-23

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: 98.93  E-value: 4.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILS-EKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSlYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERmTIIKDNH-----------------------EPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQ 745
Cdd:cd18055    81 YTGDKDSR-AIIRENEfsfddnavkggkkafkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504822311  746 TAKATRQIQAKQRFALSGTPIENRLEELWSIFQTISP-------GFLgpkKEFIQYPN-DYIRKITK---PFILRR 810
Cdd:cd18055   160 FFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPerfnnleGFL---EEFADISKeDQIKKLHDllgPHMLRR 232
DEXDc smart00487
DEAD-like helicases superfamily;
602-789 1.19e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 96.79  E-value: 1.19e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311    602 VPETLNAQLRDYQVTGFKWFKALARyqlGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAP-ASLIYNWKKEFEKF 680
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311    681 APTLSVKVVSGTKDERMTIIKD---NHEPDVWITSYPLLRQDVKLYKHMY--FDVMILDEAQAIKN--HLTQTAKATRQI 753
Cdd:smart00487   78 GPSLGLKVVGLYGGDSKREQLRkleSGKTDILVTTPGRLLDLLENDKLSLsnVDLVILDEAHRLLDggFGDQLEKLLKLL 157
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 504822311    754 -QAKQRFALSGTP---IENRLEELWSIFQTISPGFLGPKK 789
Cdd:smart00487  158 pKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
609-810 1.73e-22

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: 97.43  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  609 QLRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKI-GPSIVIAPASLIYNWKKEFEKFAPTLSVK 687
Cdd:cd18053    20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLyGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  688 VVSGTKDERMTIikDNHE----------PDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQ 757
Cdd:cd18053   100 VYLGDINSRNMI--RTHEwmhpqtkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNH 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  758 RFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQ-------YPNDYIRKITKPFILRR 810
Cdd:cd18053   178 RLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEehgkgreYGYASLHKELEPFLLRR 237
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
610-810 2.81e-22

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: 96.67  E-value: 2.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILS-EKTTEKIGPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSlYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERmTIIKDNH-----------------------EPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQ 745
Cdd:cd18057    81 YTGDKESR-SVIRENEfsfednairsgkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504822311  746 TAKATRQIQAKQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQ-----YPNDYIRKITK---PFILRR 810
Cdd:cd18057   160 FFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEefadiSKEDQIKKLHDllgPHMLRR 232
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
610-809 3.07e-22

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: 97.41  E-value: 3.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALaryqlGGILADEMGLGKTIQAISFIL--------------------------SEKTTEKIGPSIV 663
Cdd:cd18070     1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALILlhprpdndldaadddsdemvccpdclVAETPVSSKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  664 IAPASLIYNWKKEFEKFAPT-LSVKVVSGTKDERMTIIKDNH---EPDVWITSYPLLRQDV------------KLYK--- 724
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSsLKVLTYQGVKKDGALASPAPEilaEYDIVVTTYDVLRTELhyaeanrsnrrrRRQKrye 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  725 -------HMYFDVMILDEAQAIKNHLTQTAKATRQIQAKQRFALSGTPIENRLEELWSIFQtispgFLGP--------KK 789
Cdd:cd18070   156 appsplvLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLS-----FLGVepfcdsdwWA 230
                         250       260
                  ....*....|....*....|....*.
gi 504822311  790 EFIQYPN------DYIRKITKPFILR 809
Cdd:cd18070   231 RVLIRPQgrnkarEPLAALLKELLWR 256
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
610-810 2.49e-21

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: 93.92  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYNWKKEFEKFApTLSVKVV 689
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  690 SGT--------------KDERMTIIKDNHEPDVWITSYPLLRQDVKLYKHMYFDVMILDEAQAIKNHLTQTAKATRQIQA 755
Cdd:cd18061    80 HGSlisrqmiqqyemyfRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504822311  756 KQRFALSGTPIENRLEELWSIFQTISPGFLGPKKEFIQYPNDY--------IRKITKPFILRR 810
Cdd:cd18061   160 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLkteeqvqkLQAILKPMMLRR 222
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
609-1012 2.27e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 90.08  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  609 QLRDYQVTGF-KWFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIgpsIVIAP-ASLIYNWKKEFEKFaptLSV 686
Cdd:COG1061    80 ELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV---LVLVPrRELLEQWAEELRRF---LGD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  687 KVVSGTKDERmtiikdnhEPDVWITSYPLLRQDVKLYKHM-YFDVMILDEAqaiknHLTqTAKATRQI----QAKQRFAL 761
Cdd:COG1061   154 PLAGGGKKDS--------DAPITVATYQSLARRAHLDELGdRFGLVIIDEA-----HHA-GAPSYRRIleafPAAYRLGL 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  762 SGTPI-ENRLEELWSIFQTISPGFlgPKKEFIQypndyiRKITKPFILrrlktdvlpdlpekieFEQYSELTKEQKQvYL 840
Cdd:COG1061   220 TATPFrSDGREILLFLFDGIVYEY--SLKEAIE------DGYLAPPEY----------------YGIRVDLTDERAE-YD 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  841 AYLERIEQQLDAvvdanqfnqekieilagltrlrqicchpslflenyqGESGKLELLMTMIEQlRAENRRVLIFSQFSSM 920
Cdd:COG1061   275 ALSERLREALAA------------------------------------DAERKDKILRELLRE-HPDDRKTLVFCSSVDH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  921 LKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGEREIfIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAGRA 1000
Cdd:COG1061   318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRI-LVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRG 396
                         410
                  ....*....|..
gi 504822311 1001 HRIGQTKKVEVI 1012
Cdd:COG1061   397 LRPAPGKEDALV 408
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
610-810 5.46e-18

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: 83.49  E-value: 5.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKwfKALARYQLGGILADEMGLGKTIQAIsFILSEKTTE-KIGPSIVIAPASLIYNWKKEFEKFAPTLSVKV 688
Cdd:cd18011     1 PLPHQIDAVL--RALRKPPVRLLLADEVGLGKTIEAG-LIIKELLLRgDAKRVLILCPASLVEQWQDELQDKFGLPFLIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  689 VSGTKDERMTIIKDN-HEPDVWITSYPLLRQDVKLYKHMY---FDVMILDEAQAIKNhlTQTAKATRQIQAKQRFA---- 760
Cdd:cd18011    78 DRETAAQLRRLIGNPfEEFPIVIVSLDLLKRSEERRGLLLseeWDLVVVDEAHKLRN--SGGGKETKRYKLGRLLAkrar 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504822311  761 ----LSGTPIENRLEELWSIFQTISPGFLGPKKEFIQypNDYIRKITKPFILRR 810
Cdd:cd18011   156 hvllLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR--LDGLREVLAKVLLRR 207
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
610-775 1.26e-14

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: 74.31  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTGFKWFKALARYqlgGILADeMGLGKTIQAISFILSEKTTEKIGPSIVIAPASLIYN-WKKEFEKFA--PTLSV 686
Cdd:cd18013     1 PHPYQKVAINFIIEHPYC---GLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNhlRNLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  687 KVVSGTKDERMTIIkdNHEPDVWITSYPLLRQDVKLYK-HMYFDVMILDEAQAIKNHLTQTAKATRQI--QAKQRFALSG 763
Cdd:cd18013    77 SVAVGTERQRSKAA--NTPADLYVINRENLKWLVNKSGdPWPFDMVVIDELSSFKSPRSKRFKALRKVrpVIKRLIGLTG 154
                         170
                  ....*....|..
gi 504822311  764 TPIENRLEELWS 775
Cdd:cd18013   155 TPSPNGLMDLWA 166
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
884-1057 2.58e-10

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 64.75  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  884 LENYQGESGKLELLMTMIEQLRAENR--RVLIFSQFSSMLKIIEKELNKQRYQSFYLDGQTPL--------KDRVEMAEA 953
Cdd:COG1111   327 AEEADIEHPKLSKLREILKEQLGTNPdsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKegdkgltqKEQIEILER 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  954 FNNGEREIfIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAGRAHRIGQTKkveVIRLITQGTIEEKIFQLQERKRK 1033
Cdd:COG1111   407 FRAGEFNV-LVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGR---VVVLIAKGTRDEAYYWSSRRKEK 482
                         170       180
                  ....*....|....*....|....
gi 504822311 1034 LVDEIIQPGETLLSSLNEKELREL 1057
Cdd:COG1111   483 KMKSILKKLKKLLDKQEKEKLKES 506
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
610-765 1.03e-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: 58.09  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  610 LRDYQVTG-FKWFKALARYQlgGILADEMGLGKTI--QAISFILSEKTTekigpsIVIAP-ASLIYNWKKEFEKFAPTLS 685
Cdd:cd17926     1 LRPYQEEAlEAWLAHKNNRR--GILVLPTGSGKTLtaLALIAYLKELRT------LIVVPtDALLDQWKERFEDFLGDSS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  686 VKVVSGTKdermtiIKDNHEPDVWITSYPLLRQDVKLYKHMY--FDVMILDEAqaiknHLTqTAKATRQI----QAKQRF 759
Cdd:cd17926    73 IGLIGGGK------KKDFDDANVVVATYQSLSNLAEEEKDLFdqFGLLIVDEA-----HHL-PAKTFSEIlkelNAKYRL 140

                  ....*.
gi 504822311  760 ALSGTP 765
Cdd:cd17926   141 GLTATP 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
944-1015 3.64e-08

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: 51.55  E-value: 3.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504822311  944 LKDRVEMAEAFnngEREI-FIISLKAGGTGLNLTGADTVILFDLWWNPAVEAQAAGRAHRIGQtKKVEVIRLI 1015
Cdd:cd18785     9 FTNSIEHAEEI---ASSLeILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
ResIII pfam04851
Type III restriction enzyme, res subunit;
609-767 9.80e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 52.67  E-value: 9.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   609 QLRDYQVTGFK-WFKALARYQLGGILADEMGLGKTIQAISFILSEKTTEKIGPSIVIAP-ASLIYNWKKEFEKFAP--TL 684
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPnyVE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311   685 SVKVVSGTKDERmtiikDNHEPDVWITSYP----LLRQDVKLYKHMYFDVMILDEAqaikNHLtqTAKATRQI----QAK 756
Cdd:pfam04851   83 IGEIISGDKKDE-----SVDDNKIVVTTIQslykALELASLELLPDFFDVIIIDEA----HRS--GASSYRNIleyfKPA 151
                          170
                   ....*....|.
gi 504822311   757 QRFALSGTPIE 767
Cdd:pfam04851  152 FLLGLTATPER 162
DpdE NF041062
protein DpdE;
626-771 1.70e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 55.75  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  626 RYqlggILADEMGLGKTIQAiSFILSEKTTEKigPS---IVIAPASLIYNWKKEF-EKFA----PTLSVKVVSgtkderm 697
Cdd:NF041062  172 RY----LLADEVGLGKTIEA-GLVIRQHLLDN--PDarvLVLVPDALVRQWRRELrDKFFlddfPGARVRVLS------- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  698 tiikdnHE-PDVWITsypllrqdvklyKHMYFDVMILDEAQaiknHLTQTAKATRQIQaKQRFA--------------LS 762
Cdd:NF041062  238 ------HEePERWEP------------LLDAPDLLVVDEAH----QLARLAWSGDPPE-RARYRelaalahaaprlllLS 294

                  ....*....
gi 504822311  763 GTPIENRLE 771
Cdd:NF041062  295 ATPVLGNEE 303
SWIM pfam04434
SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is ...
54-91 2.15e-05

SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is predicted to be organized into two N-terminal beta-strands and a C-terminal alpha helix, thus possibly adopting a fold similar to that of the C2H2 zinc finger (pfam00096). SWIM is thought to be a versatile domain that can interact with DNA or proteins in different contexts.


Pssm-ID: 309540  Cd Length: 38  Bit Score: 42.41  E-value: 2.15e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 504822311    54 YQVSIFffEDDDLEAKCDCSAYQ-THYTCKHIAAVLLAI 91
Cdd:pfam04434    1 YRVQLD--LDGLEKASCSCPDFQlNGIPCKHALAVLLAL 37
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
892-982 1.84e-04

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 43.01  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  892 GKLELLMTMIEQLRaENRRVLIFSQFSSMLKIIEKELNKQryqsfYLDGQTPLKDRVEMAEAFNNGEREIFIISlKAGGT 971
Cdd:cd18789    34 NKLRALEELLKRHE-QGDKIIVFTDNVEALYRYAKRLLKP-----FITGETPQSEREEILQNFREGEYNTLVVS-KVGDE 106
                          90
                  ....*....|.
gi 504822311  972 GLNLTGADTVI 982
Cdd:cd18789   107 GIDLPEANVAI 117
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
891-1053 3.98e-04

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 44.13  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  891 SGKLELLMTMIEQLRAEnrRVLIFSQFSSMLKIIEKELNKQRYQSFYLDGQTPLKDRVEMAEAFNNGEREIfIISLKAGG 970
Cdd:PRK01297  320 SDKYKLLYNLVTQNPWE--RVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRV-LVATDVAG 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  971 TGLNLTGADTVILFDLwwnpavEAQAAGRAHRIGQTKkveviRLITQGTI-----EEKIFQLQERK----RKLVDEIiqP 1041
Cdd:PRK01297  397 RGIHIDGISHVINFTL------PEDPDDYVHRIGRTG-----RAGASGVSisfagEDDAFQLPEIEellgRKISCEM--P 463
                         170
                  ....*....|..
gi 504822311 1042 GETLLSSLNEKE 1053
Cdd:PRK01297  464 PAELLKPVPRKH 475
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
630-739 1.84e-03

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: 40.08  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504822311  630 GGILADEMGLGKTIQAISFILSEkTTEKIGPSIVIAP-ASLIYNWKKEF-EKFAPTLSVKVVSG--TKDERMTIIKDNhe 705
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLL-LLKKGKKVLVLVPtKALALQTAERLrELFGPGIRVAVLVGgsSAEEREKNKLGD-- 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 504822311  706 PDVWITSYPLLRQDVKLYKHMY---FDVMILDEAQAI 739
Cdd:cd00046    80 ADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHAL 116
 
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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