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Conserved domains on  [gi|15226870|ref|NP_178318|]
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SNF2 domain-containing protein / helicase domain-containing protein [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

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, ...
207-737 1.90e-128

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 398.06  E-value: 1.90e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 207 SDFQPILKPYQLVGVNFLLLLYKKGIeGAILADEMGLGKTIQAITYLTLLsRLNNDPGPHLVVCPASVLENWERELRKWC 286
Cdd:COG0553 236 AGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLEL-KERGLARPVLIVAPTSLVGNWQRELAKFA 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 287 PSFTVLQYHGAARAAysRELNSLSKAgkpppfNVLLVCYSLFerhseqqKDDRKVLKRWRWSCVLMDEAHALKDKNSYRW 366
Cdd:COG0553 314 PGLRVLVLDGTRERA--KGANPFEDA------DLVITSYGLL-------RRDIELLAAVDWDLVILDEAQHIKNPATKRA 378
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 367 KNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENV---DLKKLLNAEDTELITRMKSILGPFILRRLKSD 443
Cdd:COG0553 379 KAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAfreRFARPIEKGDEEALERLRRLLRPFLLRRTKED 456
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 444 VMQQLVPKIQRVEYVLMERKQEDAYKEAIEEYRAASQARlvKLSSKSLNSLAkALpkrqisnyfTQFRKIANHPLLirri 523
Cdd:COG0553 457 VLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGA--EGIRRRGLILA-AL---------TRLRQICSHPAL---- 520
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 524 ysdedviriarklhpigafgfecsldrVIEEVKGFNDfrihqllfqygvndtkgtlsdkhvmLSAKCRTLAELLPSMKKS 603
Cdd:COG0553 521 ---------------------------LLEEGAELSG-------------------------RSAKLEALLELLEELLAE 548
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 604 GHRVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSIFACLLSTRAGGQGLNLTGADTVIIHDM 683
Cdd:COG0553 549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 15226870 684 DFNPQIDRQAEDRCHRIGQTKPVTIFRLVTKSTVDENIYEIAKRKLVLDAAVLE 737
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
207-737 1.90e-128

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 398.06  E-value: 1.90e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 207 SDFQPILKPYQLVGVNFLLLLYKKGIeGAILADEMGLGKTIQAITYLTLLsRLNNDPGPHLVVCPASVLENWERELRKWC 286
Cdd:COG0553 236 AGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLEL-KERGLARPVLIVAPTSLVGNWQRELAKFA 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 287 PSFTVLQYHGAARAAysRELNSLSKAgkpppfNVLLVCYSLFerhseqqKDDRKVLKRWRWSCVLMDEAHALKDKNSYRW 366
Cdd:COG0553 314 PGLRVLVLDGTRERA--KGANPFEDA------DLVITSYGLL-------RRDIELLAAVDWDLVILDEAQHIKNPATKRA 378
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 367 KNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENV---DLKKLLNAEDTELITRMKSILGPFILRRLKSD 443
Cdd:COG0553 379 KAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAfreRFARPIEKGDEEALERLRRLLRPFLLRRTKED 456
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 444 VMQQLVPKIQRVEYVLMERKQEDAYKEAIEEYRAASQARlvKLSSKSLNSLAkALpkrqisnyfTQFRKIANHPLLirri 523
Cdd:COG0553 457 VLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGA--EGIRRRGLILA-AL---------TRLRQICSHPAL---- 520
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 524 ysdedviriarklhpigafgfecsldrVIEEVKGFNDfrihqllfqygvndtkgtlsdkhvmLSAKCRTLAELLPSMKKS 603
Cdd:COG0553 521 ---------------------------LLEEGAELSG-------------------------RSAKLEALLELLEELLAE 548
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 604 GHRVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSIFACLLSTRAGGQGLNLTGADTVIIHDM 683
Cdd:COG0553 549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 15226870 684 DFNPQIDRQAEDRCHRIGQTKPVTIFRLVTKSTVDENIYEIAKRKLVLDAAVLE 737
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
213-739 9.52e-107

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 350.25  E-value: 9.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYENGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   293 QYHGAARA-AYSRElnSLSKAGKpppFNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYrwknLMS 371
Cdd:PLN03142  249 KFHGNPEErAHQRE--ELLVAGK---FDVCVTSF-------EMAIKEKTALKRFSWRYIIIDEAHRIKNENSL----LSK 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   372 VAR--NANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTT-ENVDLKKLLNAED--TELITRMKSILGPFILRRLKSDVMQ 446
Cdd:PLN03142  313 TMRlfSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGENdqQEVVQQLHKVLRPFLLRRLKSDVEK 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   447 QLVPKIQRVEYVLMERKQEDAYKEAIEeyraasqarlvklssKSLNSLAKALPKRQISNYFTQFRKIANHPllirriysd 526
Cdd:PLN03142  393 GLPPKKETILKVGMSQMQKQYYKALLQ---------------KDLDVVNAGGERKRLLNIAMQLRKCCNHP--------- 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   527 edviriarklhpigafgfecsldrvieevkgfndfrihqLLFQyGVNDTKGTLSDKH-VMLSAKCRTLAELLPSMKKSGH 605
Cdd:PLN03142  449 ---------------------------------------YLFQ-GAEPGPPYTTGEHlVENSGKMVLLDKLLPKLKERDS 488
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   606 RVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKS-IFACLLSTRAGGQGLNLTGADTVIIHDMD 684
Cdd:PLN03142  489 RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSeKFVFLLSTRAGGLGINLATADIVILYDSD 568
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15226870   685 FNPQIDRQAEDRCHRIGQTKPVTIFRLVTKSTVDENIYEIAKRKLVLDAAVLESG 739
Cdd:PLN03142  569 WNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
213-406 2.51e-78

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


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 249.41  E-value: 2.51e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIeGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGP-GGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARAAYSRElnslsKAGKPPPFNVLLVCYSLFERHSEQqkddrkvLKRWRWSCVLMDEAHALKDKNSYRWKNLMSV 372
Cdd:cd17919  80 VYHGSQRERAQIR-----AKEKLDKFDVVLTTYETLRRDKAS-------LRKFRWDLVVVDEAHRLKNPKSQLSKALKAL 147
                       170       180       190
                ....*....|....*....|....*....|....
gi 15226870 373 arNANQRLMLTGTPLQNDLHELWSLLEFMLPDIF 406
Cdd:cd17919 148 --RAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
216-520 9.33e-66

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: 219.86  E-value: 9.33e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   216 YQLVGVNFLLLLYKKGIEGAILADEMGLGKTIQAITYLTLLSRLNNDPG-PHLVVCPASVLENWERELRKWC--PSFTVL 292
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   293 QYHGAARAAySRELNSLSKAGKpppFNVLLVCYSLFERHSEqqkddrkVLKRWRWSCVLMDEAHALKDKNSYrwKNLMSV 372
Cdd:pfam00176  81 VLHGNKRPQ-ERWKNDPNFLAD---FDVVITTYETLRKHKE-------LLKKVHWHRIVLDEGHRLKNSKSK--LSKALK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   373 ARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKK----LLNAEDTELITRMKSILGPFILRRLKSDVMQQL 448
Cdd:pfam00176 148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWfdrpIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226870   449 VPKIQRVEYVLMERKQEDAYKEaieeyraasqarlvKLSSKSLNSLAKAL----PKRQISNYFTQFRKIANHPLLI 520
Cdd:pfam00176 228 PPKVEYILFCRLSKLQRKLYQT--------------FLLKKDLNAIKTGEggreIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
213-412 7.46e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.13  E-value: 7.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870    213 LKPYQLVGVNFLLllykKGIEGAILADEMGLGKTIQAITYLtLLSRLNNDPGPHLVVCPASVL-ENWERELRKWCPSF-- 289
Cdd:smart00487   9 LRPYQKEAIEALL----SGLRDVILAAPTGSGKTLAALLPA-LEALKRGKGGRVLVLVPTRELaEQWAEELKKLGPSLgl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870    290 -TVLQYHGAARAAYSRELNSlskagkpPPFNVLLVCYSLFERHSEQQKDDRKvlkrwRWSCVLMDEAHALKDKNSYR-WK 367
Cdd:smart00487  84 kVVGLYGGDSKREQLRKLES-------GKTDILVTTPGRLLDLLENDKLSLS-----NVDLVILDEAHRLLDGGFGDqLE 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 15226870    368 NLMSVARNANQRLMLTGTP---LQNDLHELWSLLEFMLPDIFTTENVD 412
Cdd:smart00487 152 KLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIE 199
DpdE NF041062
protein DpdE;
237-712 6.23e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 53.05  E-value: 6.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   237 LADEMGLGKTIQAitYLTLLSRLNNDPGPH-LVVCPASVLENWERELR-KWCpsftvlqyhgaaraaysreLNSLSKAGk 314
Cdd:NF041062  175 LADEVGLGKTIEA--GLVIRQHLLDNPDARvLVLVPDALVRQWRRELRdKFF-------------------LDDFPGAR- 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   315 pppFNVLlvcyslfeRHSEQQKddrkvLKRWRWSCVLM--DEAHAL-------KDKNSYRWKNLMSVARNANQRLMLTGT 385
Cdd:NF041062  233 ---VRVL--------SHEEPER-----WEPLLDAPDLLvvDEAHQLarlawsgDPPERARYRELAALAHAAPRLLLLSAT 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   386 PLQND-------LHEL------WSLLE-------------------------FMLPDIFTtenvDLKKLLnAEDTE---L 424
Cdd:NF041062  297 PVLGNeetflalLHLLdpdlypLDDLEafrerleereelgrlvlgldpdnpnFLLRQALD----ELRALF-PEDEElqeL 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   425 ITRMKSILGPF----------------------------ILRRLKSDVMQQ--LVPKIQRVEYVLMERKQEDAYKEAIEE 474
Cdd:NF041062  372 AEELLPLLDEFddeepeeraravsalrahisetyrlhrrMIRNRRSSVLGAdyLVPGRAGPRVLVWESPAREAADEALED 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   475 YRaaSQARLVKLSSKSLnslakalpkrQISNYFTQFrkianhPLLIRRIYSDEDVIRIARKLhpigafgfecsLDRVIEE 554
Cdd:NF041062  452 WR--EEAALLDAESDPA----------ARAAYARAL------AWLVARLGGPDDLAALLRWR-----------LRGDAAS 502
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   555 VkgfnDFRIHQLLFQYGVNDTKGTLSDKHVMlsakcRTLAELLPSMKKSGHRVLIFSQWTSMLDILEWTLDVIGVT--YR 632
Cdd:NF041062  503 A----DLAGERELLEALIAALEDEAKDADLL-----AALADWLLPLLRGSGKAVVFCGDGSLADHLAAALARLGAGsvER 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   633 RLDGSTqVTDRQTIVDTFNNDKSIfACLLSTRAGGQGLNLTGADTVIIHDMDFNPQ-----IDRQaeDRCHRIGQTKPVT 707
Cdd:NF041062  574 HLSGQG-ADQAERAVRAFRQDPSA-RVLVCDRSGEEGLNLQGADRLVHLDLPWSPNrleqrIGRL--DRYASLRGGRPVE 649

                  ....*
gi 15226870   708 IFRLV 712
Cdd:NF041062  650 SYVLA 654
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
207-737 1.90e-128

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 398.06  E-value: 1.90e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 207 SDFQPILKPYQLVGVNFLLLLYKKGIeGAILADEMGLGKTIQAITYLTLLsRLNNDPGPHLVVCPASVLENWERELRKWC 286
Cdd:COG0553 236 AGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLEL-KERGLARPVLIVAPTSLVGNWQRELAKFA 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 287 PSFTVLQYHGAARAAysRELNSLSKAgkpppfNVLLVCYSLFerhseqqKDDRKVLKRWRWSCVLMDEAHALKDKNSYRW 366
Cdd:COG0553 314 PGLRVLVLDGTRERA--KGANPFEDA------DLVITSYGLL-------RRDIELLAAVDWDLVILDEAQHIKNPATKRA 378
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 367 KNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENV---DLKKLLNAEDTELITRMKSILGPFILRRLKSD 443
Cdd:COG0553 379 KAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAfreRFARPIEKGDEEALERLRRLLRPFLLRRTKED 456
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 444 VMQQLVPKIQRVEYVLMERKQEDAYKEAIEEYRAASQARlvKLSSKSLNSLAkALpkrqisnyfTQFRKIANHPLLirri 523
Cdd:COG0553 457 VLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGA--EGIRRRGLILA-AL---------TRLRQICSHPAL---- 520
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 524 ysdedviriarklhpigafgfecsldrVIEEVKGFNDfrihqllfqygvndtkgtlsdkhvmLSAKCRTLAELLPSMKKS 603
Cdd:COG0553 521 ---------------------------LLEEGAELSG-------------------------RSAKLEALLELLEELLAE 548
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 604 GHRVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSIFACLLSTRAGGQGLNLTGADTVIIHDM 683
Cdd:COG0553 549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 15226870 684 DFNPQIDRQAEDRCHRIGQTKPVTIFRLVTKSTVDENIYEIAKRKLVLDAAVLE 737
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
213-739 9.52e-107

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 350.25  E-value: 9.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYENGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   293 QYHGAARA-AYSRElnSLSKAGKpppFNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYrwknLMS 371
Cdd:PLN03142  249 KFHGNPEErAHQRE--ELLVAGK---FDVCVTSF-------EMAIKEKTALKRFSWRYIIIDEAHRIKNENSL----LSK 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   372 VAR--NANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTT-ENVDLKKLLNAED--TELITRMKSILGPFILRRLKSDVMQ 446
Cdd:PLN03142  313 TMRlfSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGENdqQEVVQQLHKVLRPFLLRRLKSDVEK 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   447 QLVPKIQRVEYVLMERKQEDAYKEAIEeyraasqarlvklssKSLNSLAKALPKRQISNYFTQFRKIANHPllirriysd 526
Cdd:PLN03142  393 GLPPKKETILKVGMSQMQKQYYKALLQ---------------KDLDVVNAGGERKRLLNIAMQLRKCCNHP--------- 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   527 edviriarklhpigafgfecsldrvieevkgfndfrihqLLFQyGVNDTKGTLSDKH-VMLSAKCRTLAELLPSMKKSGH 605
Cdd:PLN03142  449 ---------------------------------------YLFQ-GAEPGPPYTTGEHlVENSGKMVLLDKLLPKLKERDS 488
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   606 RVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKS-IFACLLSTRAGGQGLNLTGADTVIIHDMD 684
Cdd:PLN03142  489 RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSeKFVFLLSTRAGGLGINLATADIVILYDSD 568
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15226870   685 FNPQIDRQAEDRCHRIGQTKPVTIFRLVTKSTVDENIYEIAKRKLVLDAAVLESG 739
Cdd:PLN03142  569 WNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
213-406 2.51e-78

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


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 249.41  E-value: 2.51e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIeGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGP-GGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARAAYSRElnslsKAGKPPPFNVLLVCYSLFERHSEQqkddrkvLKRWRWSCVLMDEAHALKDKNSYRWKNLMSV 372
Cdd:cd17919  80 VYHGSQRERAQIR-----AKEKLDKFDVVLTTYETLRRDKAS-------LRKFRWDLVVVDEAHRLKNPKSQLSKALKAL 147
                       170       180       190
                ....*....|....*....|....*....|....
gi 15226870 373 arNANQRLMLTGTPLQNDLHELWSLLEFMLPDIF 406
Cdd:cd17919 148 --RAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
213-439 1.58e-67

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: 222.23  E-value: 1.58e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18003   1 LREYQHIGLDWLATLYEKNLNG-ILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARAAYsrelnsLSKAG--KPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLM 370
Cdd:cd18003  80 TYYGSAKERK------LKRQGwmKPNSFHVCITSYQLVVQ-------DHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 371 SVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFtTENVDLKKLLN-----------AEDTELITRMKSILGPFILRR 439
Cdd:cd18003 147 NF--NTQRRLLLTGTPLQNSLMELWSLMHFLMPHIF-QSHQEFKEWFSnpltamsegsqEENEELVRRLHKVLRPFLLRR 223
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
213-406 5.01e-66

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: 216.87  E-value: 5.01e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLsRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd17998   1 LKDYQLIGLNWLNLLYQKKLSG-ILADEMGLGKTIQVIAFLAYL-KEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARA-AYSRElNSLSKAGKpppFNVLLVCYSLferhSEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLMS 371
Cdd:cd17998  79 PYYGSQEErKHLRY-DILKGLED---FDVIVTTYNL----ATSNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15226870 372 VarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIF 406
Cdd:cd17998 151 I--NANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
216-520 9.33e-66

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: 219.86  E-value: 9.33e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   216 YQLVGVNFLLLLYKKGIEGAILADEMGLGKTIQAITYLTLLSRLNNDPG-PHLVVCPASVLENWERELRKWC--PSFTVL 292
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   293 QYHGAARAAySRELNSLSKAGKpppFNVLLVCYSLFERHSEqqkddrkVLKRWRWSCVLMDEAHALKDKNSYrwKNLMSV 372
Cdd:pfam00176  81 VLHGNKRPQ-ERWKNDPNFLAD---FDVVITTYETLRKHKE-------LLKKVHWHRIVLDEGHRLKNSKSK--LSKALK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   373 ARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKK----LLNAEDTELITRMKSILGPFILRRLKSDVMQQL 448
Cdd:pfam00176 148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWfdrpIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226870   449 VPKIQRVEYVLMERKQEDAYKEaieeyraasqarlvKLSSKSLNSLAKAL----PKRQISNYFTQFRKIANHPLLI 520
Cdd:pfam00176 228 PPKVEYILFCRLSKLQRKLYQT--------------FLLKKDLNAIKTGEggreIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
213-441 2.35e-64

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: 213.72  E-value: 2.35e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd17997   4 MRDYQIRGLNWLISLFENGING-ILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGA--ARAAYSRELNslskagKPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSyrwkNLM 370
Cdd:cd17997  83 VLIGDkeERADIIRDVL------LPGKFDVCITSYEMVIK-------EKTVLKKFNWRYIIIDEAHRIKNEKS----KLS 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226870 371 SVAR--NANQRLMLTGTPLQNDLHELWSLLEFMLPDIFT-TENVD----LKKLLNAEDtELITRMKSILGPFILRRLK 441
Cdd:cd17997 146 QIVRlfNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTsSEDFDewfnVNNCDDDNQ-EVVQRLHKVLRPFLLRRIK 222
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
579-712 2.19e-62

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: 205.02  E-value: 2.19e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 579 LSDKHVM-LSAKCRTLAELLPSMKKSGHRVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSIF 657
Cdd:cd18793   1 LPPKIEEvVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIR 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15226870 658 ACLLSTRAGGQGLNLTGADTVIIHDMDFNPQIDRQAEDRCHRIGQTKPVTIFRLV 712
Cdd:cd18793  81 VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
212-441 2.38e-58

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: 197.99  E-value: 2.38e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 212 ILKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLsRLNNDPGPHLVVCPASVLENWERELRKWCPSFTV 291
Cdd:cd18009   3 VMRPYQLEGMEWLRMLWENGING-ILADEMGLGKTIQTIALLAHL-RERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 292 LQYHGAA--RAAYSRELNSlsKAGKPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNL 369
Cdd:cd18009  81 LLYHGTKeeRERLRKKIMK--REGTLQDFPVVVTSYEIAMR-------DRKALQHYAWKYLIVDEGHRLKNLNCRLIQEL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 370 MSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFT--------------TENVDLKKLLNAEDTELITRM-KSILGP 434
Cdd:cd18009 152 KTF--NSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDdlssfeswfdfsslSDNAADISNLSEEREQNIVHMlHAILKP 229

                ....*..
gi 15226870 435 FILRRLK 441
Cdd:cd18009 230 FLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
213-441 3.45e-58

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: 197.59  E-value: 3.45e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd17996   4 LKEYQLKGLQWMVSLYNNNLNG-ILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHG--AARaaysRELNSLSKAGKpppFNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSyRWKNLM 370
Cdd:cd17996  83 VYKGtpDVR----KKLQSQIRAGK---FNVLLTTY-------EYIIKDKPLLSKIKWKYMIIDEGHRMKNAQS-KLTQTL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 371 SVARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIF--------------TTENVDLKKLLNAEDTEL-ITRMKSILGPF 435
Cdd:cd17996 148 NTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFkscktfeqwfntpfANTGEQVKIELNEEETLLiIRRLHKVLRPF 227

                ....*.
gi 15226870 436 ILRRLK 441
Cdd:cd17996 228 LLRRLK 233
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
209-441 1.03e-57

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: 195.86  E-value: 1.03e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 209 FQPILKPYQLVGVNFLLLLYKKGIeGAILADEMGLGKTIQAITYLtLLSRLNNDPGPHLVVCPASVLENWERELRKWCPS 288
Cdd:cd18012   1 LKATLRPYQKEGFNWLSFLRHYGL-GGILADDMGLGKTLQTLALL-LSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 289 FTVLQYHGAARAaySRELNSLSKAgkpppfNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSYRWKN 368
Cdd:cd18012  79 LKVLVIHGTKRK--REKLRALEDY------DLVITSYGLLRR-------DIELLKEVKFHYLVLDEAQNIKNPQTKTAKA 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226870 369 LMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKK----LLNAEDTELITRMKSILGPFILRRLK 441
Cdd:cd18012 144 VKAL--KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRfakpIEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
213-439 6.87e-56

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: 190.73  E-value: 6.87e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKkGIEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18006   1 LRPYQLEGVNWLLQCRA-EQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHG--AARAAYSRELNSLskagkpPPFNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNL- 369
Cdd:cd18006  80 TYMGdkEKRLDLQQDIKST------NRFHVLLTTY-------EICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLs 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226870 370 -MSVARnanqRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDlkKLLNA-----EDTELITRMKSILGPFILRR 439
Cdd:cd18006 147 eFSVDF----RLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLD--DFIKAysetdDESETVEELHLLLQPFLLRR 216
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
213-439 8.29e-55

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: 188.10  E-value: 8.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18002   1 LKEYQLKGLNWLANLYEQGING-ILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAA--RAAYSRELNSLSKAGKPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLM 370
Cdd:cd18002  80 PYWGNPkdRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQ-------DEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 371 SVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTEN-------VDLKKllNAE-----DTELITRMKSILGPFILR 438
Cdd:cd18002 153 SF--HCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDefnewfsKDIES--HAEnktglNEHQLKRLHMILKPFMLR 228

                .
gi 15226870 439 R 439
Cdd:cd18002 229 R 229
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
213-439 1.52e-54

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: 187.18  E-value: 1.52e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGiEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd17993   2 LRDYQLTGLNWLAHSWCKG-NNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARA-AYSRELNSLSKAGKPPPFNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLMS 371
Cdd:cd17993  81 VYLGDIKSrDTIREYEFYFSQTKKLKFNVLLTTY-------EIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226870 372 VarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENvDLKKLLNAEDTELITRMKSILGPFILRR 439
Cdd:cd17993 154 F--KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWE-EFEEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
213-439 7.67e-51

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: 177.06  E-value: 7.67e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGiEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPsFTVL 292
Cdd:cd17995   1 LRDYQLEGVNWLLFNWYNR-RNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGaarAAYSRELNSLSK-----AGKPPP-----FNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKN 362
Cdd:cd17995  79 VYHG---SGESRQIIQQYEmyfkdAQGRKKkgvykFDVLITTYEMVIA-------DAEELRKIPWRVVVVDEAHRLKNRN 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226870 363 SYRWKNLMSVARnaNQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFILRR 439
Cdd:cd17995 149 SKLLQGLKKLTL--EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
213-451 1.31e-48

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: 171.77  E-value: 1.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18064  16 LRDYQVRGLNWLISLYENGING-ILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHG--AARAAYSRELNslskagKPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSyrwkNLM 370
Cdd:cd18064  95 CLIGdkDQRAAFVRDVL------LPGEWDVCVTSYEMLIK-------EKSVFKKFNWRYLVIDEAHRIKNEKS----KLS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 371 SVAR--NANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENvDLKKLLNAE----DTELITRMKSILGPFILRRLKSDV 444
Cdd:cd18064 158 EIVRefKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAE-DFDSWFDTNnclgDQKLVERLHMVLRPFLLRRIKADV 236

                ....*..
gi 15226870 445 MQQLVPK 451
Cdd:cd18064 237 EKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
213-441 8.42e-47

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: 166.35  E-value: 8.42e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18065  16 LRDYQVRGLNWMISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHG--AARAAYSRELNslskagKPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSyrwkNLM 370
Cdd:cd18065  95 CLIGdkDARAAFIRDVM------MPGEWDVCVTSYEMVIK-------EKSVFKKFNWRYLVIDEAHRIKNEKS----KLS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226870 371 SVAR--NANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTEN-----VDLKKLLNaeDTELITRMKSILGPFILRRLK 441
Cdd:cd18065 158 EIVRefKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADdfdswFDTKNCLG--DQKLVERLHAVLKPFLLRRIK 233
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
213-439 5.58e-46

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: 162.61  E-value: 5.58e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEgAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd17994   1 LHPYQLEGLNWLRFSWAQGTD-TILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAaraaysrelnslskagkpppfNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLMSV 372
Cdd:cd17994  80 TYVGD---------------------HVLLTSYELISI-------DQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSY 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226870 373 arNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFILRR 439
Cdd:cd17994 132 --KIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
213-439 7.70e-44

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: 157.92  E-value: 7.70e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGiEGAILADEMGLGKTIQAITYLTLL--SRLNNDPgphLVVCPASVLENWERELRKWCPSFT 290
Cdd:cd18001   1 LYPHQREGVAWLWSLHDGG-KGGILADDMGLGKTVQICAFLSGMfdSGLIKSV---LVVMPTSLIPHWVKEFAKWTPGLR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 291 VLQYHGAARAAYSRELNSLSKAGkpppfNVLLVCYSLFERHSEQQKDDRKvlKRWRWSCVLMDEAHALKDKNSYRWKNLM 370
Cdd:cd18001  77 VKVFHGTSKKERERNLERIQRGG-----GVLLTTYGMVLSNTEQLSADDH--DEFKWDYVILDEGHKIKNSKTKSAKSLR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 371 SVarNANQRLMLTGTPLQNDLHELWSLLEF-----MLPDIFTTENVDLKKLLNAED-----------TELITRMKSILGP 434
Cdd:cd18001 150 EI--PAKNRIILTGTPIQNNLKELWALFDFacngsLLGTRKTFKMEFENPITRGRDkdatqgekalgSEVAENLRQIIKP 227

                ....*
gi 15226870 435 FILRR 439
Cdd:cd18001 228 YFLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
213-439 1.61e-43

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: 157.47  E-value: 1.61e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGiEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18054  21 LRDYQLEGLNWLAHSWCKN-NSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARAAYS-RELNSLSKAGKPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLMS 371
Cdd:cd18054 100 VYIGDLMSRNTiREYEWIHSQTKRLKFNALITTYEILLK-------DKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLID 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226870 372 VarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTT----ENVDLKKLLNAEDTelitrMKSILGPFILRR 439
Cdd:cd18054 173 F--KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFwedfEEDHGKGRENGYQS-----LHKVLEPFLLRR 237
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
212-441 1.03e-42

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: 155.59  E-value: 1.03e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 212 ILKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTV 291
Cdd:cd18062  23 VLKQYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 292 LQYHG--AARAAYSRELNSlskaGKpppFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSyRWKNL 369
Cdd:cd18062 102 VSYKGspAARRAFVPQLRS----GK---FNVLLTTYEYIIK-------DKQILAKIRWKYMIVDEGHRMKNHHC-KLTQV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 370 MSVARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIF----------------TTENVDlkklLNAEDTELIT-RMKSIL 432
Cdd:cd18062 167 LNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFkscstfeqwfnapfamTGEKVD----LNEEETILIIrRLHKVL 242

                ....*....
gi 15226870 433 GPFILRRLK 441
Cdd:cd18062 243 RPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
213-441 1.57e-42

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: 155.22  E-value: 1.57e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18063  24 LKHYQLQGLEWMVSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKI 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAarAAYSRELNSLSKAGKpppFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSyRWKNLMSV 372
Cdd:cd18063 103 SYKGT--PAMRRSLVPQLRSGK---FNVLLTTYEYIIK-------DKHILAKIRWKYMIVDEGHRMKNHHC-KLTQVLNT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 373 ARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIF----------------TTENVDlkklLNAEDTELIT-RMKSILGPF 435
Cdd:cd18063 170 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFkscstfeqwfnapfamTGERVD----LNEEETILIIrRLHKVLRPF 245

                ....*.
gi 15226870 436 ILRRLK 441
Cdd:cd18063 246 LLRRLK 251
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
213-403 4.08e-40

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: 146.31  E-value: 4.08e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIeGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSF--T 290
Cdd:cd18000   1 LFKYQQTGVQWLWELHCQRV-GGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFrvV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 291 VLQYHGAARAA----YSRELNSLSKAGKPPPFNVLLVCYSLFERHSeqqkddrKVLKRWRWSCVLMDEAHALKDKN---S 363
Cdd:cd18000  80 VLHSSGSGTGSeeklGSIERKSQLIRKVVGDGGILITTYEGFRKHK-------DLLLNHNWQYVILDEGHKIRNPDaeiT 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15226870 364 YRWKNLMSVarnanQRLMLTGTPLQNDLHELWSLLEFMLP 403
Cdd:cd18000 153 LACKQLRTP-----HRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
213-439 4.31e-40

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: 147.11  E-value: 4.31e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLL-LYKKgiEGAILADEMGLGKTIQAITYLTLLSrLNNDPGPHLVVCPASVLENWERELRKWCpSFTV 291
Cdd:cd18058   1 LREYQLEGMNWLLFnWYNR--KNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWT-EMNA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 292 LQYHGAA---RAAYSRELNSLSKAGKPPP----FNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSY 364
Cdd:cd18058  77 IVYHGSQisrQMIQQYEMYYRDEQGNPLSgifkFQVVITTF-------EMILADCPELKKINWSCVIIDEAHRLKNRNCK 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226870 365 RWKNLMSVArnANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFILRR 439
Cdd:cd18058 150 LLEGLKLMA--LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
213-439 7.98e-40

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: 147.14  E-value: 7.98e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGiEGAILADEMGLGKTIQAITYLTLL--------------------SRLNNDPGPHLVVCPA 272
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNG-RGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprfkkkPPASSAKKPVLIVAPL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 273 SVLENWERELRKWcPSFTVLQYHGAARAaysRELNSLSKAGKpppFNVLLVCYSLFERHSEQqkddrkvLKRWRWSCVLM 352
Cdd:cd18005  80 SVLYNWKDELDTW-GHFEVGVYHGSRKD---DELEGRLKAGR---LEVVVTTYDTLRRCIDS-------LNSINWSAVIA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 353 DEAHALKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLP------DIFTTENVDLKKL---LNAEDTE 423
Cdd:cd18005 146 DEAHRIKNPKSKLTQAMKEL--KCKVRIGLTGTLLQNNMKELWCLLDWAVPgalgsrSQFKKHFSEPIKRgqrHTATARE 223
                       250       260
                ....*....|....*....|..
gi 15226870 424 L------ITRMKSILGPFILRR 439
Cdd:cd18005 224 LrlgrkrKQELAVKLSKFFLRR 245
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
213-439 8.99e-40

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


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 146.66  E-value: 8.99e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLllykkgIEGAILADEMGLGKTIQAI-----------------TYLTLLSRLNNDPGPHLVVCPASVL 275
Cdd:cd18008   1 LLPYQKQGLAWML------PRGGILADEMGLGKTIQALalilatrpqdpkipeelEENSSDPKKLYLSKTTLIVVPLSLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 276 ENWERELRK--WCPSFTVLQYHGAARAAYSRELNSlskagkpppFNVLLVCYSLFERHSEQQKDDRKV---------LKR 344
Cdd:cd18008  75 SQWKDEIEKhtKPGSLKVYVYHGSKRIKSIEELSD---------YDIVITTYGTLASEFPKNKKGGGRdskekeaspLHR 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 345 WRWSCVLMDEAHALKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTE---NVDLKKLLNAED 421
Cdd:cd18008 146 IRWYRVILDEAHNIKNRSTKTSRAVCAL--KAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYpwfNSDISKPFSKND 223
                       250
                ....*....|....*...
gi 15226870 422 TELITRMKSILGPFILRR 439
Cdd:cd18008 224 RKALERLQALLKPILLRR 241
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
213-439 1.02e-39

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: 146.36  E-value: 1.02e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEgAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18057   1 LHPYQLEGLNWLRFSWAQGTD-TILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARA-------AYSRELNSLSKAGK--------PPPFNVLLVCYSLFerhseqqKDDRKVLKRWRWSCVLMDEAHA 357
Cdd:cd18057  80 TYTGDKESrsvirenEFSFEDNAIRSGKKvfrmkkeaQIKFHVLLTSYELI-------TIDQAILGSIEWACLVVDEAHR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 358 LKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFIL 437
Cdd:cd18057 153 LKNNQSKFFRVLNSY--KIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHML 230

                ..
gi 15226870 438 RR 439
Cdd:cd18057 231 RR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
213-439 4.39e-39

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: 144.77  E-value: 4.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEgAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18055   1 LHMYQLEGLNWLRFSWAQGTD-TILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHG--AARA-----AYSRELNSLsKAGK---------PPPFNVLLVCYSLFerhseqqKDDRKVLKRWRWSCVLMDEAH 356
Cdd:cd18055  80 TYTGdkDSRAiirenEFSFDDNAV-KGGKkafkmkreaQVKFHVLLTSYELV-------TIDQAALGSIRWACLVVDEAH 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 357 ALKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFI 436
Cdd:cd18055 152 RLKNNQSKFFRVLNGY--KIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHM 229

                ...
gi 15226870 437 LRR 439
Cdd:cd18055 230 LRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
213-439 1.61e-38

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: 143.20  E-value: 1.61e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLL--LLYKK--GIEGAILADEMGLGKTIQAITYL-TLLSRLNNDPGPH---LVVCPASVLENWERELRK 284
Cdd:cd18004   1 LRPHQREGVQFLYdcLTGRRgyGGGGAILADEMGLGKTLQAIALVwTLLKQGPYGKPTAkkaLIVCPSSLVGNWKAEFDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 285 WCPS--FTVLQYHGAARAAYSRELNSLSkagkPPPFNVLLVCYSLFERHSEQQKDDRkvlkrwrwSCVLM--DEAHALKD 360
Cdd:cd18004  81 WLGLrrIKVVTADGNAKDVKASLDFFSS----ASTYPVLIISYETLRRHAEKLSKKI--------SIDLLicDEGHRLKN 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 361 KNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTT--------ENVDLKKLL---NAEDTEL-ITRM 428
Cdd:cd18004 149 SESKTTKALNSL--PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSlasfrkvfEEPILRSRDpdaSEEDKELgAERS 226
                       250
                ....*....|....
gi 15226870 429 K---SILGPFILRR 439
Cdd:cd18004 227 QelsELTSRFILRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
213-409 9.16e-37

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: 138.19  E-value: 9.16e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFL---LLLYKKGIE---GAILADEMGLGKTIQAITYL-TLLSRLNNDPGPhLVVCPASVLENWERELRKW 285
Cdd:cd18007   1 LKPHQVEGVRFLwsnLVGTDVGSDeggGCILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 286 CPSFTVLQYHGAARAAYSRELNSLSKagkpppFN-------VLLVCYSLFER-HSEQQKDDRKVLKRWRWSC------VL 351
Cdd:cd18007  80 LPPDLRPLLVLVSLSASKRADARLRK------INkwhkeggVLLIGYELFRNlASNATTDPRLKQEFIAALLdpgpdlLV 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15226870 352 MDEAHALKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTE 409
Cdd:cd18007 154 LDEGHRLKNEKSQLSKALSKV--KTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTL 209
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
213-439 3.39e-36

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: 135.93  E-value: 3.39e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKgIEGAILADEMGLGKTIQAITYLTLLSrLNNDPGPHLVVCPASVLENWERELRKWCpSFTVL 292
Cdd:cd18059   1 LREYQLEGVNWLLFNWYN-TRNCILADEMGLGKTIQSITFLYEIY-LKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAAraAYSRELNSLSKAGKPPPFNVLLVCYSLFERHS--EQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLM 370
Cdd:cd18059  78 VYHGSQ--ASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITtfEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226870 371 SVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFILRR 439
Cdd:cd18059 156 MM--DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
213-439 5.12e-36

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: 135.57  E-value: 5.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLL-LYKKgiEGAILADEMGLGKTIQAITYLTLLSRLNNDpGPHLVVCPASVLENWERELRKWCPSFTV 291
Cdd:cd18060   1 LREYQLEGVNWLLFnWYNR--QNCILADEMGLGKTIQSIAFLQEVYNVGIH-GPFLVIAPLSTITNWEREFNTWTEMNTI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 292 LqYHG--AARAAYSR-ELNSLSKAGKPPP----FNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSY 364
Cdd:cd18060  78 V-YHGslASRQMIQQyEMYCKDSRGRLIPgaykFDALITTF-------EMILSDCPELREIEWRCVIIDEAHRLKNRNCK 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226870 365 RWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFILRR 439
Cdd:cd18060 150 LLDSLKHM--DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
213-439 7.56e-36

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: 135.58  E-value: 7.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEgAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18056   1 LHPYQLEGLNWLRFSWAQGTD-TILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHG--AARA-----AYSRELNSLSKAGKPP--------PFNVLLVCYSLFerhseqqKDDRKVLKRWRWSCVLMDEAHA 357
Cdd:cd18056  80 TYVGdkDSRAiirenEFSFEDNAIRGGKKASrmkkeasvKFHVLLTSYELI-------TIDMAILGSIDWACLIVDEAHR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 358 LKDKNSYRWKNLMSVArnANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFIL 437
Cdd:cd18056 153 LKNNQSKFFRVLNGYS--LQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHML 230

                ..
gi 15226870 438 RR 439
Cdd:cd18056 231 RR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
213-439 8.01e-36

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: 135.56  E-value: 8.01e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGiEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVL 292
Cdd:cd18053  21 LRDYQLNGLNWLAHSWCKG-NSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARAA-YSRELNSLSKAGKPPPFNVLLVCYSLFERhseqqkdDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLMS 371
Cdd:cd18053 100 VYLGDINSRnMIRTHEWMHPQTKRLKFNILLTTYEILLK-------DKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLID 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226870 372 VarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSiLGPFILRR 439
Cdd:cd18053 173 F--KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKE-LEPFLLRR 237
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
213-439 1.52e-35

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: 134.40  E-value: 1.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGaILADEMGLGKTIQAITYLTLLSRL-----NNDPGPHLVVCPASVLENWERELRKWCP 287
Cdd:cd17999   1 LRPYQQEGINWLAFLNKYNLHG-ILCDDMGLGKTLQTLCILASDHHKransfNSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 288 SF--TVLQYHGAArAAYSRELNSLSKAgkpppfNVLLVCYslferhsEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYR 365
Cdd:cd17999  80 NAflKPLAYVGPP-QERRRLREQGEKH------NVIVASY-------DVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 366 WKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENV----DLKKLL-------NAEDTEL----ITRM-K 429
Cdd:cd17999 146 SKAVKQL--KANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQfqrrFLKPILasrdskaSAKEQEAgalaLEALhK 223
                       250
                ....*....|
gi 15226870 430 SILgPFILRR 439
Cdd:cd17999 224 QVL-PFLLRR 232
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
213-410 1.44e-33

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: 128.09  E-value: 1.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLllYKKGieGAILADEMGLGKTIQAITyltLLSRLNNDpGPHLVVCPASVLENWERELRKWCPSFTVl 292
Cdd:cd18010   1 LLPFQREGVCFAL--RRGG--RVLIADEMGLGKTVQAIA---IAAYYREE-WPLLIVCPSSLRLTWADEIERWLPSLPP- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 qyhgaaraaysRELNSLSKAG---KPPPFNVLLVCYSLFERHSEQqkddrkvLKRWRWSCVLMDEAHALKDKNSYRWKNL 369
Cdd:cd18010  72 -----------DDIQVIVKSKdglRDGDAKVVIVSYDLLRRLEKQ-------LLARKFKVVICDESHYLKNSKAKRTKAA 133
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15226870 370 MSVARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTEN 410
Cdd:cd18010 134 LPLLKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFH 174
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
213-439 3.07e-32

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: 124.73  E-value: 3.07e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLL-LYKKgiEGAILADEMGLGKTIQAITYLTLLSRlNNDPGPHLVVCPASVLENWERELRKWCpSFTV 291
Cdd:cd18061   1 LREYQLEGLNWLLFnWYNR--RNCILADEMGLGKTIQSITFLYEILL-TGIRGPFLIIAPLSTIANWEREFRTWT-DLNV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 292 LQYHGAA---RAAYSRELNSLSKAGK----PPPFNVLLVCYSLFERHSEQqkddrkvLKRWRWSCVLMDEAHALKDKNSY 364
Cdd:cd18061  77 VVYHGSLisrQMIQQYEMYFRDSQGRiirgAYRFQAIITTFEMILGGCPE-------LNAIDWRCVIIDEAHRLKNKNCK 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226870 365 RWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFILRR 439
Cdd:cd18061 150 LLEGLKLM--NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
213-439 6.58e-32

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: 124.50  E-value: 6.58e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLlllYK-------KGIEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHL----VVCPASVLENWERE 281
Cdd:cd18067   1 LRPHQREGVKFL---YRcvtgrriRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 282 LRKWC-PSFTVLQYHGAARAAYSREL-NSLSKAGKPPPFNVLLVCYSLFERHSEQqkddrkvLKRWRWSCVLMDEAHALK 359
Cdd:cd18067  78 LGKWLgGRLQPLAIDGGSKKEIDRKLvQWASQQGRRVSTPVLIISYETFRLHVEV-------LQKGEVGLVICDEGHRLK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 360 DKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTT-----ENVDLKKL-------LNAEDTELITR 427
Cdd:cd18067 151 NSDNQTYQALDSL--NTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTaaefkKNFELPILkgrdadaSEKERQLGEEK 228
                       250
                ....*....|....*
gi 15226870 428 MK---SILGPFILRR 439
Cdd:cd18067 229 LQeliSIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
213-439 2.07e-29

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 116.87  E-value: 2.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFL----LLLYKKGIEGAILADEMGLGKTIQAITYLTLLSRLNNDPGP-----HLVVCPASVLENWERELR 283
Cdd:cd18066   1 LRPHQREGIEFLyecvMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKpvikrALIVTPGSLVKNWKKEFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 284 KWCPS-----FTVLQYHGAARAAYSrelnslskagkpPPFNVLLVCYSLFERHSEQqkddrkvLKRWRWSCVLMDEAHAL 358
Cdd:cd18066  81 KWLGSerikvFTVDQDHKVEEFIAS------------PLYSVLIISYEMLLRSLDQ-------ISKLNFDLVICDEGHRL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 359 KDKNSYRWKNLMSVArnANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENV-------------------DLKKLLNA 419
Cdd:cd18066 142 KNTSIKTTTALTSLS--CERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTyrkvyeepivrsreptatpEEKKLGEA 219
                       250       260
                ....*....|....*....|
gi 15226870 420 EDTELiTRMksiLGPFILRR 439
Cdd:cd18066 220 RAAEL-TRL---TGLFILRR 235
DEXDc smart00487
DEAD-like helicases superfamily;
213-412 7.46e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.13  E-value: 7.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870    213 LKPYQLVGVNFLLllykKGIEGAILADEMGLGKTIQAITYLtLLSRLNNDPGPHLVVCPASVL-ENWERELRKWCPSF-- 289
Cdd:smart00487   9 LRPYQKEAIEALL----SGLRDVILAAPTGSGKTLAALLPA-LEALKRGKGGRVLVLVPTRELaEQWAEELKKLGPSLgl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870    290 -TVLQYHGAARAAYSRELNSlskagkpPPFNVLLVCYSLFERHSEQQKDDRKvlkrwRWSCVLMDEAHALKDKNSYR-WK 367
Cdd:smart00487  84 kVVGLYGGDSKREQLRKLES-------GKTDILVTTPGRLLDLLENDKLSLS-----NVDLVILDEAHRLLDGGFGDqLE 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 15226870    368 NLMSVARNANQRLMLTGTP---LQNDLHELWSLLEFMLPDIFTTENVD 412
Cdd:smart00487 152 KLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIE 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
588-701 1.12e-26

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: 104.99  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   588 AKCRTLAELLPsmKKSGHRVLIFSQWTSMLDIlEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSIFacLLSTRAGG 667
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV--LVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 15226870   668 QGLNLTGADTVIIHDMDFNPQIDRQAEDRCHRIG 701
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
213-407 1.26e-25

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: 105.06  E-value: 1.26e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLlykKGIEGAILADEMGLGKTIQAITYLTLLsRLNNDPGPHLVVCPASVLENWERELRKwcpsftvl 292
Cdd:cd18011   1 PLPHQIDAVLRALR---KPPVRLLLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELQD-------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 293 QYHGAARAAYSRELNSLSKAGKPPPFNVLLVCYSLFERHSeqQKDDRKVLKRWRWSCVLMDEAHALKDKN----SYRWKN 368
Cdd:cd18011  69 KFGLPFLILDRETAAQLRRLIGNPFEEFPIVIVSLDLLKR--SEERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKL 146
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15226870 369 LMSVARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFT 407
Cdd:cd18011 147 GRLLAKRARHVLLLTATPHNGKEEDFRALLSLLDPGRFA 185
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
234-401 1.52e-24

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: 102.93  E-value: 1.52e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 234 GAILADEMGLGKTIQAITYLtllsrLNNdpgPHLVVCPASVLENWERELRKWCPS--FTVLQYHGAARaaySRELNSLSK 311
Cdd:cd18071  50 GGILADDMGLGKTLTTISLI-----LAN---FTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHGGER---NRDPKLLSK 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 312 agkpppFNVLLVCYSLFErHSEQQKDDRKvLKRWRWSCVLMDEAHALKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDL 391
Cdd:cd18071 119 ------YDIVLTTYNTLA-SDFGAKGDSP-LHTINWLRVVLDEGHQIRNPNAQQTKAVLNL--SSERRWVLTGTPIQNSP 188
                       170
                ....*....|
gi 15226870 392 HELWSLLEFM 401
Cdd:cd18071 189 KDLGSLLSFL 198
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
213-439 1.29e-21

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 94.47  E-value: 1.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLYKKGIEGAILADEMGLGKTIQAITyLTLLSRLNND-----------------------PGPHLVV 269
Cdd:cd18072   1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIA-LILAQKNTQNrkeeekekalteweskkdstlvpSAGTLVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 270 CPASVLENWERELRKWCPS--FTVLQYHGAARAAYSRELNSlskagkpppFNVLLVCYSLFERHSEQQKDDRKV--LKRW 345
Cdd:cd18072  80 CPASLVHQWKNEVESRVASnkLRVCLYHGPNRERIGEVLRD---------YDIVITTYSLVAKEIPTYKEESRSspLFRI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 346 RWSCVLMDEAHALKDKNSyrwKNLMSVAR-NANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVdLKKLLNAEDTEL 424
Cdd:cd18072 151 AWARIILDEAHNIKNPKV---QASIAVCKlRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKV-WKKQVDNKSRKG 226
                       250
                ....*....|....*
gi 15226870 425 ITRMKSILGPFILRR 439
Cdd:cd18072 227 GERLNILTKSLLLRR 241
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
213-408 1.16e-19

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: 88.72  E-value: 1.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLlllYKKGIE-----------GAILADEMGLGKTIQAITYLTLLSRlNNDPGPHLVVCPASVLENWERE 281
Cdd:cd18069   1 LKPHQIGGIRFL---YDNIIEslerykgssgfGCILAHSMGLGKTLQVISFLDVLLR-HTGAKTVLAIVPVNTLQNWLSE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 282 LRKWCPSFT-------------VLQYHGAARAAYSRELNSLSKAGkpppfNVLLVCYSLFerhseQQKDDRKVlkrwrws 348
Cdd:cd18069  77 FNKWLPPPEalpnvrprpfkvfILNDEHKTTAARAKVIEDWVKDG-----GVLLMGYEMF-----RLRPGPDV------- 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 349 cVLMDEAHALKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTT 408
Cdd:cd18069 140 -VICDEGHRIKNCHASTSQALKNI--RSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGT 196
HELICc smart00490
helicase superfamily c-terminal domain;
618-701 2.89e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 2.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870    618 DILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSIFacLLSTRAGGQGLNLTGADTVIIHDMDFNPQIDRQAEDRC 697
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV--LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 15226870    698 HRIG 701
Cdd:smart00490  79 GRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
213-408 4.97e-19

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: 87.25  E-value: 4.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNF--------LLLLYKKGIEGAILADEMGLGKTIQAITYL--TLLSRLNNDPGPHLVVCPASVLENWEREL 282
Cdd:cd18068   1 LKPHQVDGVQFmwdcccesLKKTKKSPGSGCILAHCMGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 283 RKWcpsftvlqyHGAARAAYSRELNSLSKAGKPPP--------FN---VLLVCYSLFE--------RHSEQQKDD-RKVL 342
Cdd:cd18068  81 EKW---------QEGLKDEEKIEVNELATYKRPQErsyklqrwQEeggVMIIGYDMYRilaqernvKSREKLKEIfNKAL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226870 343 KRWRWSCVLMDEAHALKDKNSYRWKNLMSVarNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTT 408
Cdd:cd18068 152 VDPGPDFVVCDEGHILKNEASAVSKAMNSI--RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGT 215
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
213-396 1.60e-17

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: 82.01  E-value: 1.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLllykKGIEGAILADeMGLGKTIQAITYLTLLsRLNNDPGPHLVVCPASVLEN-WERELRKW--CPSF 289
Cdd:cd18013   1 PHPYQKVAINFII----EHPYCGLFLD-MGLGKTVTTLTALSDL-QLDDFTRRVLVIAPLRVARStWPDEVEKWnhLRNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 290 TVLQYHGAARAaysrelnsLSKAGKPPPfnvllvcySLFERHSEQQKD-DRKVLKRWRWSCVLMDEAHALKDKNSYRWKN 368
Cdd:cd18013  75 TVSVAVGTERQ--------RSKAANTPA--------DLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKA 138
                       170       180
                ....*....|....*....|....*...
gi 15226870 369 LMSVARNANQRLMLTGTPLQNDLHELWS 396
Cdd:cd18013 139 LRKVRPVIKRLIGLTGTPSPNGLMDLWA 166
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
213-407 2.07e-15

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 77.00  E-value: 2.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 213 LKPYQLVGVNFLLLLykkgieGAILADEMGLGKTIQAITyLTLLSRLNNDP--------------------------GPH 266
Cdd:cd18070   1 LLPYQRRAVNWMLVP------GGILADEMGLGKTVEVLA-LILLHPRPDNDldaadddsdemvccpdclvaetpvssKAT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 267 LVVCPASVLENWERELRKWCP-SFTVLQYHGAaraaysrelNSLSKAGKPPP------------FNVLL--VCYSLFERH 331
Cdd:cd18070  74 LIVCPSAILAQWLDEINRHVPsSLKVLTYQGV---------KKDGALASPAPeilaeydivvttYDVLRteLHYAEANRS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 332 SEQQKDDRKV------LKRWRWSCVLMDEAHALKDKNSyrwkNLMSVARN--ANQRLMLTGTPLQNDLHELWSLLEFMLP 403
Cdd:cd18070 145 NRRRRRQKRYeappspLVLVEWWRVCLDEAQMVESSTS----KAAEMARRlpRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220

                ....
gi 15226870 404 DIFT 407
Cdd:cd18070 221 EPFC 224
DpdE NF041062
protein DpdE;
237-712 6.23e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 53.05  E-value: 6.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   237 LADEMGLGKTIQAitYLTLLSRLNNDPGPH-LVVCPASVLENWERELR-KWCpsftvlqyhgaaraaysreLNSLSKAGk 314
Cdd:NF041062  175 LADEVGLGKTIEA--GLVIRQHLLDNPDARvLVLVPDALVRQWRRELRdKFF-------------------LDDFPGAR- 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   315 pppFNVLlvcyslfeRHSEQQKddrkvLKRWRWSCVLM--DEAHAL-------KDKNSYRWKNLMSVARNANQRLMLTGT 385
Cdd:NF041062  233 ---VRVL--------SHEEPER-----WEPLLDAPDLLvvDEAHQLarlawsgDPPERARYRELAALAHAAPRLLLLSAT 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   386 PLQND-------LHEL------WSLLE-------------------------FMLPDIFTtenvDLKKLLnAEDTE---L 424
Cdd:NF041062  297 PVLGNeetflalLHLLdpdlypLDDLEafrerleereelgrlvlgldpdnpnFLLRQALD----ELRALF-PEDEElqeL 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   425 ITRMKSILGPF----------------------------ILRRLKSDVMQQ--LVPKIQRVEYVLMERKQEDAYKEAIEE 474
Cdd:NF041062  372 AEELLPLLDEFddeepeeraravsalrahisetyrlhrrMIRNRRSSVLGAdyLVPGRAGPRVLVWESPAREAADEALED 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   475 YRaaSQARLVKLSSKSLnslakalpkrQISNYFTQFrkianhPLLIRRIYSDEDVIRIARKLhpigafgfecsLDRVIEE 554
Cdd:NF041062  452 WR--EEAALLDAESDPA----------ARAAYARAL------AWLVARLGGPDDLAALLRWR-----------LRGDAAS 502
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   555 VkgfnDFRIHQLLFQYGVNDTKGTLSDKHVMlsakcRTLAELLPSMKKSGHRVLIFSQWTSMLDILEWTLDVIGVT--YR 632
Cdd:NF041062  503 A----DLAGERELLEALIAALEDEAKDADLL-----AALADWLLPLLRGSGKAVVFCGDGSLADHLAAALARLGAGsvER 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   633 RLDGSTqVTDRQTIVDTFNNDKSIfACLLSTRAGGQGLNLTGADTVIIHDMDFNPQ-----IDRQaeDRCHRIGQTKPVT 707
Cdd:NF041062  574 HLSGQG-ADQAERAVRAFRQDPSA-RVLVCDRSGEEGLNLQGADRLVHLDLPWSPNrleqrIGRL--DRYASLRGGRPVE 649

                  ....*
gi 15226870   708 IFRLV 712
Cdd:NF041062  650 SYVLA 654
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
233-360 6.50e-05

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: 43.55  E-value: 6.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 233 EGAILADEMGLGKTIQAitYLTLLSRLNNDPGPHLVVCPASVLEN-WERELRKWCPSFTVLQYHGAARAAYSRELNSLSK 311
Cdd:cd00046   2 ENVLITAPTGSGKTLAA--LLAALLLLLKKGKKVLVLVPTKALALqTAERLRELFGPGIRVAVLVGGSSAEEREKNKLGD 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15226870 312 AgkpppfNVLLVCYSLFERHSEQqkDDRKVLKRWRWscVLMDEAHALKD 360
Cdd:cd00046  80 A------DIIIATPDMLLNLLLR--EDRLFLKDLKL--IIVDEAHALLI 118
PTZ00110 PTZ00110
helicase; Provisional
593-703 7.39e-04

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 42.84  E-value: 7.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870  593 LAELLPSMKKSGHRVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSifACLLSTRAGGQGLNL 672
Cdd:PTZ00110 366 LKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKS--PIMIATDVASRGLDV 443
                         90       100       110
                 ....*....|....*....|....*....|.
gi 15226870  673 TGADTVIihDMDFNPQIdrqaEDRCHRIGQT 703
Cdd:PTZ00110 444 KDVKYVI--NFDFPNQI----EDYVHRIGRT 468
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
205-443 2.69e-03

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 41.16  E-value: 2.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 205 EDSDFQPILKPYQLVGVNFLLLLYKKGIEGAILADEMGLGKTI---QAITYLTLLSRLnndpgphLVVCP-ASVLENWER 280
Cdd:COG1061  73 EASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVlalALAAELLRGKRV-------LVLVPrRELLEQWAE 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 281 ELRKWCPSFTVLQYHgaaraaysrelnslskagKPPPFNVLLVCYSLFERHseqqkDDRKVLKRwRWSCVLMDEAHALkd 360
Cdd:COG1061 146 ELRRFLGDPLAGGGK------------------KDSDAPITVATYQSLARR-----AHLDELGD-RFGLVIIDEAHHA-- 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 361 kNSYRWKNLMSvARNANQRLMLTGTPLQNDLHElwsLLEFMLPDIftTENVDLKKLLNAEdtelitrmksILGPFILRRL 440
Cdd:COG1061 200 -GAPSYRRILE-AFPAAYRLGLTATPFRSDGRE---ILLFLFDGI--VYEYSLKEAIEDG----------YLAPPEYYGI 262

                ...
gi 15226870 441 KSD 443
Cdd:COG1061 263 RVD 265
HgdB COG1775
Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB [Amino acid ...
291-399 3.54e-03

Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441381  Cd Length: 384  Bit Score: 40.27  E-value: 3.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870 291 VLQYHGAARAAYsRELNSLSKAgKPPP---FNVLLVCYSLF----ERHSEQQKDdrkvlkrwrwscvLMDEahaLKDkns 363
Cdd:COG1775 166 AIKLYNEARKLL-RELYELRKA-KPPPisgFDLLLVMAAAFfmdkEEATELLEE-------------LLDE---LEE--- 224
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15226870 364 yRWKNLMSVARNANQRLMLTGTPLQNDLHELWSLLE 399
Cdd:COG1775 225 -RIAEGIGAVPEEKPRILWTGIPPWPPNRKLLKLIE 259
ResIII pfam04851
Type III restriction enzyme, res subunit;
213-386 6.33e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   213 LKPYQLVGVNFLLLLYKKGIEGAILADEMGLGKTI---QAITYLTLLSRLNNdpgpHLVVCP-ASVLENWERELRKWCPS 288
Cdd:pfam04851   4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLtaaKLIARLFKKGPIKK----VLFLVPrKDLLEQALEEFKKFLPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226870   289 ftvlqYHGAaraaySRELNSLSKAGKPPPFNVLLVCYSLFERHSEQQKDDrkvLKRWRWSCVLMDEAHALKDKNsyrWKN 368
Cdd:pfam04851  80 -----YVEI-----GEIISGDKKDESVDDNKIVVTTIQSLYKALELASLE---LLPDFFDVIIIDEAHRSGASS---YRN 143
                         170
                  ....*....|....*...
gi 15226870   369 LMSvARNANQRLMLTGTP 386
Cdd:pfam04851 144 ILE-YFKPAFLLGLTATP 160
 
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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