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Conserved domains on  [gi|66812928|ref|XP_640643|]
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SNF2-related domain-containing protein [Dictyostelium discoideum AX4]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12785020)

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

CATH:  3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0004386|GO:0005524
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 345-553 4.50e-102

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: 318.77  E-value: 4.50e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGRCLIADDMGLGKTIQGISIAYHYKEEWPLLIIAPSSLRLVWADQIEKFFPNkIQSSEINLVMN 424
Cdd:cd18010    1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPS-LPPDDIQVIVK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  425 GKCGLNGM---INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVLKRSKRCILLSGTPALSRPMELF 501
Cdd:cd18010   80 SKDGLRDGdakVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66812928  502 IQISCINP-YFMQWRDYAFRYCAAFQEKFCFNTSGCSNMKEL-NLYLNTFMIRR 553
Cdd:cd18010  160 TQLDALDPkLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELhLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 344-784 1.38e-87

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.98  E-value: 1.38e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISIAYHYKEE---WPLLIIAPSSLRLVWADQIEKFFPnkiqss 417
Cdd:COG0553  241 TLRPYQLEGAAwllFLRRLGLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAP------ 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  418 EIN-LVMNGKCGLNGMIN--------IISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKStAEVLKrSKRCILL 488
Cdd:COG0553  315 GLRvLVLDGTRERAKGANpfedadlvITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKA-VRALK-ARHRLAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  489 SGTPALSRPMELFIQISCINPYFMQwrDYAfrycaAFQEKFCF--NTSGCSNMKELNLYLNTFMIRRLKDDVMTELPEKR 566
Cdd:COG0553  393 TGTPVENRLEELWSLLDFLNPGLLG--SLK-----AFRERFARpiEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  567 RERILVKLDKtklkevqktlveinQHRKVYLDPNTDMKTSF---KNKNSRQGLFFKLLR------DTGLY---------- 627
Cdd:COG0553  466 EETLYVELTP--------------EQRALYEAVLEYLRRELegaEGIRRRGLILAALTRlrqicsHPALLleegaelsgr 531

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  628 --KLTAVTQFLKEkLVDApiDQKFLIFAHHKEvingivhMLGKIK--VDKKKLEFIKIDGSTPAQNRNDYVNDFQNDPNC 703
Cdd:COG0553  532 saKLEALLELLEE-LLAE--GEKVLVFSQFTD-------TLDLLEerLEERGIEYAYLHGGTSAEERDELVDRFQEGPEA 601

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  704 RVAVLSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYGQTSSVLVQYLIALGTVDEMIWSLVESKKTLLGRVL 783
Cdd:COG0553  602 PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681


                 .
gi 66812928  784 D 784
Cdd:COG0553  682 G 682
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 345-553 4.50e-102

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: 318.77  E-value: 4.50e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGRCLIADDMGLGKTIQGISIAYHYKEEWPLLIIAPSSLRLVWADQIEKFFPNkIQSSEINLVMN 424
Cdd:cd18010    1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPS-LPPDDIQVIVK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  425 GKCGLNGM---INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVLKRSKRCILLSGTPALSRPMELF 501
Cdd:cd18010   80 SKDGLRDGdakVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66812928  502 IQISCINP-YFMQWRDYAFRYCAAFQEKFCFNTSGCSNMKEL-NLYLNTFMIRR 553
Cdd:cd18010  160 TQLDALDPkLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELhLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 344-784 1.38e-87

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.98  E-value: 1.38e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISIAYHYKEE---WPLLIIAPSSLRLVWADQIEKFFPnkiqss 417
Cdd:COG0553  241 TLRPYQLEGAAwllFLRRLGLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAP------ 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  418 EIN-LVMNGKCGLNGMIN--------IISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKStAEVLKrSKRCILL 488
Cdd:COG0553  315 GLRvLVLDGTRERAKGANpfedadlvITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKA-VRALK-ARHRLAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  489 SGTPALSRPMELFIQISCINPYFMQwrDYAfrycaAFQEKFCF--NTSGCSNMKELNLYLNTFMIRRLKDDVMTELPEKR 566
Cdd:COG0553  393 TGTPVENRLEELWSLLDFLNPGLLG--SLK-----AFRERFARpiEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  567 RERILVKLDKtklkevqktlveinQHRKVYLDPNTDMKTSF---KNKNSRQGLFFKLLR------DTGLY---------- 627
Cdd:COG0553  466 EETLYVELTP--------------EQRALYEAVLEYLRRELegaEGIRRRGLILAALTRlrqicsHPALLleegaelsgr 531

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  628 --KLTAVTQFLKEkLVDApiDQKFLIFAHHKEvingivhMLGKIK--VDKKKLEFIKIDGSTPAQNRNDYVNDFQNDPNC 703
Cdd:COG0553  532 saKLEALLELLEE-LLAE--GEKVLVFSQFTD-------TLDLLEerLEERGIEYAYLHGGTSAEERDELVDRFQEGPEA 601

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  704 RVAVLSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYGQTSSVLVQYLIALGTVDEMIWSLVESKKTLLGRVL 783
Cdd:COG0553  602 PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681


                 .
gi 66812928  784 D 784
Cdd:COG0553  682 G 682
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 628-759 1.06e-41

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: 149.16  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  628 KLTAVTQFLKEKLVDapiDQKFLIFAHHKEVINGIVHMLgkikvDKKKLEFIKIDGSTPAQNRNDYVNDFQNDPNCRVAV 707
Cdd:cd18793   12 KLEALLELLEELREP---GEKVLIFSQFTDTLDILEEAL-----RERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 66812928  708 LSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYGQTSSVLVQYLI 759
Cdd:cd18793   84 LSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 363-623 4.44e-27

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: 112.39  E-value: 4.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    363 CLIADDMGLGKTIQGISI---AYHYKEEW--PLLIIAPSSLRLVWADQIEKFFPN--------KIQSSEINLVMNGKCGL 429
Cdd:pfam00176   20 GILADEMGLGKTLQTISLllyLKHVDKNWggPTLIVVPLSLLHNWMNEFERWVSPpalrvvvlHGNKRPQERWKNDPNFL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    430 NGM-INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKsTAEVLKRSKRcILLSGTPALSRPMELFIQISCIN 508
Cdd:pfam00176  100 ADFdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSK-ALKSLKTRNR-WILTGTPLQNNLEELWALLNFLR 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    509 P-------YFMQWRDyafrycaafqekFCFNTSGC-SNMKELNLYLNTFMIRRLKDDVMTELPEKRRERILVKLDKtklk 580
Cdd:pfam00176  178 PgpfgslsTFRNWFD------------RPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSK---- 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 66812928    581 evqktlveinQHRKVY----LDPNTD-MKTSFKNKNSRQGLFFKLLRD 623
Cdd:pfam00176  242 ----------LQRKLYqtflLKKDLNaIKTGEGGREIKASLLNILMRL 279
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 348-844 1.00e-24

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 111.43  E-value: 1.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   348 FQIKGIEFGI---EKGGRCLIADDMGLGKTIQGISIAYHYKE----EWPLLIIAPSSLRLVWADQIEKFFP--------- 411
Cdd:PLN03142  173 YQLAGLNWLIrlyENGINGILADEMGLGKTLQTISLLGYLHEyrgiTGPHMVVAPKSTLGNWMNEIRRFCPvlravkfhg 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   412 NKIQSSEI--NLVMNGKCGlngmINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKsTAEVLKRSKRcILLS 489
Cdd:PLN03142  253 NPEERAHQreELLVAGKFD----VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSK-TMRLFSTNYR-LLIT 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   490 GTPALSRPMELFIQISCINPYFmqwrdyaFRYCAAFQEkfCFNTSGCSNMKE----LNLYLNTFMIRRLKDDVMTELPEK 565
Cdd:PLN03142  327 GTPLQNNLHELWALLNFLLPEI-------FSSAETFDE--WFQISGENDQQEvvqqLHKVLRPFLLRRLKSDVEKGLPPK 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   566 rRERILvKLDKTKLKE------VQKTLVEINQ--HRKVYLDPNTDMKTSFKNKNSRQGL-----FFK---LLRDTG-LYK 628
Cdd:PLN03142  398 -KETIL-KVGMSQMQKqyykalLQKDLDVVNAggERKRLLNIAMQLRKCCNHPYLFQGAepgppYTTgehLVENSGkMVL 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   629 LTAVTQFLKEKlvdapiDQKFLIFAHHKEVINgivhmlgkIKVDK---KKLEFIKIDGSTPAQNRNDYVNDFqNDPNCR- 704
Cdd:PLN03142  476 LDKLLPKLKER------DSRVLIFSQMTRLLD--------ILEDYlmyRGYQYCRIDGNTGGEDRDASIDAF-NKPGSEk 540

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   705 -VAVLSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYGQTSSVLVQYLIALGTVDEMIWSLVESKKTLLGRVL 783
Cdd:PLN03142  541 fVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66812928   784 DD---EDGQSLNAEDAGQL-EHGEQSV---------DDFIDSLIKKVEEQdqirKKKYDDKQRRKEEKLLKLQL 844
Cdd:PLN03142  621 QQgrlAEQKTVNKDELLQMvRYGAEMVfsskdstitDEDIDRIIAKGEEA----TAELDAKMKKFTEDAIKFKM 690
DEXDc smart00487
DEAD-like helicases superfamily;
341-512 1.94e-17

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 81.77  E-value: 1.94e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928     341 LPSTLLPFQIKGIEFGIEKGGRCLIADDMGLGKTIQ-GISIAYHYKEE--WPLLIIAP-SSLRLVWADQIEKFFPNK--- 413
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAaLLPALEALKRGkgGRVLVLVPtRELAEQWAEELKKLGPSLglk 84

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928     414 --------IQSSEINLVMNGKCGlngmINIISYDLVTK--KKDQILQKNFKVVIADECHYIKqfNSQRSKSTAEVLKR-- 481
Cdd:smart00487   85 vvglyggdSKREQLRKLESGKTD----ILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLL--DGGFGDQLEKLLKLlp 158

                           170       180       190
                    ....*....|....*....|....*....|..
gi 66812928     482 -SKRCILLSGTPalSRPMELFIQISCINPYFM 512
Cdd:smart00487  159 kNVQLLLLSATP--PEEIENLLELFLNDPVFI 188
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 628-748 2.98e-15

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: 72.63  E-value: 2.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    628 KLTAVTQFLKEKlvdapIDQKFLIFAHHKEVINgiVHMLGKikvdKKKLEFIKIDGSTPAQNRNDYVNDFqNDPNCRVaV 707
Cdd:pfam00271    2 KLEALLELLKKE-----RGGKVLIFSQTKKTLE--AELLLE----KEGIKVARLHGDLSQEEREEILEDF-RKGKIDV-L 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 66812928    708 LSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYG 748
Cdd:pfam00271   69 VATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
673-748 6.19e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.93  E-value: 6.19e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66812928     673 KKKLEFIKIDGSTPAQNRNDYVNDFQNDPNcrVAVLSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYG 748
Cdd:smart00490    9 ELGIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 345-553 4.50e-102

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: 318.77  E-value: 4.50e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGRCLIADDMGLGKTIQGISIAYHYKEEWPLLIIAPSSLRLVWADQIEKFFPNkIQSSEINLVMN 424
Cdd:cd18010    1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPS-LPPDDIQVIVK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  425 GKCGLNGM---INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVLKRSKRCILLSGTPALSRPMELF 501
Cdd:cd18010   80 SKDGLRDGdakVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66812928  502 IQISCINP-YFMQWRDYAFRYCAAFQEKFCFNTSGCSNMKEL-NLYLNTFMIRR 553
Cdd:cd18010  160 TQLDALDPkLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELhLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 344-784 1.38e-87

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.98  E-value: 1.38e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISIAYHYKEE---WPLLIIAPSSLRLVWADQIEKFFPnkiqss 417
Cdd:COG0553  241 TLRPYQLEGAAwllFLRRLGLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAP------ 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  418 EIN-LVMNGKCGLNGMIN--------IISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKStAEVLKrSKRCILL 488
Cdd:COG0553  315 GLRvLVLDGTRERAKGANpfedadlvITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKA-VRALK-ARHRLAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  489 SGTPALSRPMELFIQISCINPYFMQwrDYAfrycaAFQEKFCF--NTSGCSNMKELNLYLNTFMIRRLKDDVMTELPEKR 566
Cdd:COG0553  393 TGTPVENRLEELWSLLDFLNPGLLG--SLK-----AFRERFARpiEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  567 RERILVKLDKtklkevqktlveinQHRKVYLDPNTDMKTSF---KNKNSRQGLFFKLLR------DTGLY---------- 627
Cdd:COG0553  466 EETLYVELTP--------------EQRALYEAVLEYLRRELegaEGIRRRGLILAALTRlrqicsHPALLleegaelsgr 531

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  628 --KLTAVTQFLKEkLVDApiDQKFLIFAHHKEvingivhMLGKIK--VDKKKLEFIKIDGSTPAQNRNDYVNDFQNDPNC 703
Cdd:COG0553  532 saKLEALLELLEE-LLAE--GEKVLVFSQFTD-------TLDLLEerLEERGIEYAYLHGGTSAEERDELVDRFQEGPEA 601

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  704 RVAVLSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYGQTSSVLVQYLIALGTVDEMIWSLVESKKTLLGRVL 783
Cdd:COG0553  602 PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681


                 .
gi 66812928  784 D 784
Cdd:COG0553  682 G 682
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 628-759 1.06e-41

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: 149.16  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  628 KLTAVTQFLKEKLVDapiDQKFLIFAHHKEVINGIVHMLgkikvDKKKLEFIKIDGSTPAQNRNDYVNDFQNDPNCRVAV 707
Cdd:cd18793   12 KLEALLELLEELREP---GEKVLIFSQFTDTLDILEEAL-----RERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 66812928  708 LSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYGQTSSVLVQYLI 759
Cdd:cd18793   84 LSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 345-515 2.73e-36

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: 135.39  E-value: 2.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF---GIEKGGRCLIADDMGLGKTIQGISIAYHYKEE----WPLLIIAPSSLRLVWADQIEKFFPN----K 413
Cdd:cd17919    1 LRPYQLEGLNFlleLYENGPGGILADEMGLGKTLQAIAFLAYLLKEgkerGPVLVVCPLSVLENWEREFEKWTPDlrvvV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  414 IQSS--EINLVMNGKCGLNGMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKstaeVLK--RSKRCILLS 489
Cdd:cd17919   81 YHGSqrERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSK----ALKalRAKRRLLLT 156

                        170       180
                 ....*....|....*....|....*.
gi 66812928  490 GTPALSRPMELFIQISCINPYFMqWR 515
Cdd:cd17919  157 GTPLQNNLEELWALLDFLDPPFL-LR 181
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 363-623 4.44e-27

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: 112.39  E-value: 4.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    363 CLIADDMGLGKTIQGISI---AYHYKEEW--PLLIIAPSSLRLVWADQIEKFFPN--------KIQSSEINLVMNGKCGL 429
Cdd:pfam00176   20 GILADEMGLGKTLQTISLllyLKHVDKNWggPTLIVVPLSLLHNWMNEFERWVSPpalrvvvlHGNKRPQERWKNDPNFL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    430 NGM-INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKsTAEVLKRSKRcILLSGTPALSRPMELFIQISCIN 508
Cdd:pfam00176  100 ADFdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSK-ALKSLKTRNR-WILTGTPLQNNLEELWALLNFLR 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    509 P-------YFMQWRDyafrycaafqekFCFNTSGC-SNMKELNLYLNTFMIRRLKDDVMTELPEKRRERILVKLDKtklk 580
Cdd:pfam00176  178 PgpfgslsTFRNWFD------------RPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSK---- 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 66812928    581 evqktlveinQHRKVY----LDPNTD-MKTSFKNKNSRQGLFFKLLRD 623
Cdd:pfam00176  242 ----------LQRKLYqtflLKKDLNaIKTGEGGREIKASLLNILMRL 279
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 344-555 9.36e-25

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: 103.41  E-value: 9.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIE---FGIEKG-GRCLiADDMGLGKTIQGISIAYHYKEEW---PLLIIAPSSLRLVWADQIEKFFPnkiqs 416
Cdd:cd18012    4 TLRPYQKEGFNwlsFLRHYGlGGIL-ADDMGLGKTLQTLALLLSRKEEGrkgPSLVVAPTSLIYNWEEEAAKFAP----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  417 sEIN-LVMNGKCGLNGMIN--------IISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRSKRCIL 487
Cdd:cd18012   78 -ELKvLVIHGTKRKREKLRaledydlvITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL--KADHRLA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66812928  488 LSGTPALSRPMELFIQISCINP-YFMQWRDyafrycaaFQEKFCF---NTSGCSNMKELNLYLNTFMIRRLK 555
Cdd:cd18012  155 LTGTPIENHLGELWSIFDFLNPgLLGSYKR--------FKKRFAKpieKDGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 348-844 1.00e-24

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 111.43  E-value: 1.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   348 FQIKGIEFGI---EKGGRCLIADDMGLGKTIQGISIAYHYKE----EWPLLIIAPSSLRLVWADQIEKFFP--------- 411
Cdd:PLN03142  173 YQLAGLNWLIrlyENGINGILADEMGLGKTLQTISLLGYLHEyrgiTGPHMVVAPKSTLGNWMNEIRRFCPvlravkfhg 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   412 NKIQSSEI--NLVMNGKCGlngmINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKsTAEVLKRSKRcILLS 489
Cdd:PLN03142  253 NPEERAHQreELLVAGKFD----VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSK-TMRLFSTNYR-LLIT 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   490 GTPALSRPMELFIQISCINPYFmqwrdyaFRYCAAFQEkfCFNTSGCSNMKE----LNLYLNTFMIRRLKDDVMTELPEK 565
Cdd:PLN03142  327 GTPLQNNLHELWALLNFLLPEI-------FSSAETFDE--WFQISGENDQQEvvqqLHKVLRPFLLRRLKSDVEKGLPPK 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   566 rRERILvKLDKTKLKE------VQKTLVEINQ--HRKVYLDPNTDMKTSFKNKNSRQGL-----FFK---LLRDTG-LYK 628
Cdd:PLN03142  398 -KETIL-KVGMSQMQKqyykalLQKDLDVVNAggERKRLLNIAMQLRKCCNHPYLFQGAepgppYTTgehLVENSGkMVL 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   629 LTAVTQFLKEKlvdapiDQKFLIFAHHKEVINgivhmlgkIKVDK---KKLEFIKIDGSTPAQNRNDYVNDFqNDPNCR- 704
Cdd:PLN03142  476 LDKLLPKLKER------DSRVLIFSQMTRLLD--------ILEDYlmyRGYQYCRIDGNTGGEDRDASIDAF-NKPGSEk 540

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928   705 -VAVLSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYGQTSSVLVQYLIALGTVDEMIWSLVESKKTLLGRVL 783
Cdd:PLN03142  541 fVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66812928   784 DD---EDGQSLNAEDAGQL-EHGEQSV---------DDFIDSLIKKVEEQdqirKKKYDDKQRRKEEKLLKLQL 844
Cdd:PLN03142  621 QQgrlAEQKTVNKDELLQMvRYGAEMVfsskdstitDEDIDRIIAKGEEA----TAELDAKMKKFTEDAIKFKM 690
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 345-516 1.94e-23

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: 99.29  E-value: 1.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKG-GRCLIADDMGLGKTIQGISIAyhyKEEW------PLLIIAPSSLRLVWADQIEKFFPNKIQSS 417
Cdd:cd18011    1 PLPHQIDAVLRALRKPpVRLLLADEVGLGKTIEAGLII---KELLlrgdakRVLILCPASLVEQWQDELQDKFGLPFLIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  418 -----EINLVMNGKCGLNGMINIISYDLV---TKKKDQILQKNFKVVIADECHYI--KQFN--SQRSKSTAEVLKRSKRC 485
Cdd:cd18011   78 dretaAQLRRLIGNPFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLrnSGGGkeTKRYKLGRLLAKRARHV 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 66812928  486 ILLSGTPALSRPMELFIQISCINPYFMQWRD 516
Cdd:cd18011  158 LLLTATPHNGKEEDFRALLSLLDPGRFAVLG 188
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 345-492 1.47e-20

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: 91.97  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF----------GIEKGGRCLIADDMGLGKTIQGISIAY----HYKEEWPLLIIAPSSLRLVWADQIEKFF 410
Cdd:cd18007    1 LKPHQVEGVRFlwsnlvgtdvGSDEGGGCILAHTMGLGKTLQVITFLHtylaAAPRRSRPLVLCPASTLYNWEDEFKKWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  411 PNKIQSSEINLVMNGKCGLNG---MIN---------IISYDLVTK------KKDQILQKNFK--------VVIADECHYI 464
Cdd:cd18007   81 PPDLRPLLVLVSLSASKRADArlrKINkwhkeggvlLIGYELFRNlasnatTDPRLKQEFIAalldpgpdLLVLDEGHRL 160

                        170       180
                 ....*....|....*....|....*...
gi 66812928  465 KQFNSQRSKSTAEVlkRSKRCILLSGTP 492
Cdd:cd18007  161 KNEKSQLSKALSKV--KTKRRILLTGTP 186
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 358-500 2.83e-19

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: 87.79  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  358 EKGGRCLIADDMGLGKTIQGISIAYH---YKEEW-PLLIIAPSSLRLVWADQIEKFFPN-KIQS-----SEINLVMNGKC 427
Cdd:cd18003   17 EKNLNGILADEMGLGKTIQTIALLAHlacEKGNWgPHLIVVPTSVMLNWEMEFKRWCPGfKILTyygsaKERKLKRQGWM 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66812928  428 GLNGM-INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRSKRCILLSGTPALSRPMEL 500
Cdd:cd18003   97 KPNSFhVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNF--NTQRRLLLTGTPLQNSLMEL 168
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 345-500 6.75e-18

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: 83.94  E-value: 6.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISI----AYHYKEEW-----PLLIIAPSSLRLVWADQIEKFFPN 412
Cdd:cd17999    1 LRPYQQEGINwlaFLNKYNLHGILCDDMGLGKTLQTLCIlasdHHKRANSFnsenlPSLVVCPPTLVGHWVAEIKKYFPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  413 KIQS------SEINLVMNGKCGLNGMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRSKRCI 486
Cdd:cd17999   81 AFLKplayvgPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQL--KANHRL 158

                        170
                 ....*....|....
gi 66812928  487 LLSGTPALSRPMEL 500
Cdd:cd17999  159 ILSGTPIQNNVLEL 172
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 347-504 1.33e-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: 82.78  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  347 PFQIKGIEFGIEKGGRCLIADdMGLGKTIQGISIAYHYKEEW---PLLIIAPSSL-RLVWADQIEKF-FPNKIQSSEInl 421
Cdd:cd18013    3 PYQKVAINFIIEHPYCGLFLD-MGLGKTVTTLTALSDLQLDDftrRVLVIAPLRVaRSTWPDEVEKWnHLRNLTVSVA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  422 VMNGK-----CGLNGMINIISYDLVTKKKDQILQK-NFKVVIADECHYIKQFNSQRSKSTAEVLKRSKRCILLSGTPALS 495
Cdd:cd18013   80 VGTERqrskaANTPADLYVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIGLTGTPSPN 159


                 ....*....
gi 66812928  496 RPMELFIQI 504
Cdd:cd18013  160 GLMDLWAQI 168
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 345-553 1.48e-17

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: 83.10  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF--------GIEKGGRCLIADDMGLGKTIQGISIAY----HYKEEWPL----LIIAPSSLRLVWADQIEK 408
Cdd:cd18004    1 LRPHQREGVQFlydcltgrRGYGGGGAILADEMGLGKTLQAIALVWtllkQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  409 FFPNK------IQSSEInlvmNGKCGLNGM-------INIISYDLVTKKKDQILQK-NFKVVIADECHYIKQFNSQRSKS 474
Cdd:cd18004   81 WLGLRrikvvtADGNAK----DVKASLDFFssastypVLIISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSESKTTKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  475 TAEVlkRSKRCILLSGTPALSRPMELFIQISCINP-----------YFMQwRDYAFRYCAAFQEKfcfNTSGCSNMKELN 543
Cdd:cd18004  157 LNSL--PCRRRLLLTGTPIQNDLDEFFALVDFVNPgilgslasfrkVFEE-PILRSRDPDASEED---KELGAERSQELS 230

                        250
                 ....*....|
gi 66812928  544 LYLNTFMIRR 553
Cdd:cd18004  231 ELTSRFILRR 240
DEXDc smart00487
DEAD-like helicases superfamily;
341-512 1.94e-17

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 81.77  E-value: 1.94e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928     341 LPSTLLPFQIKGIEFGIEKGGRCLIADDMGLGKTIQ-GISIAYHYKEE--WPLLIIAP-SSLRLVWADQIEKFFPNK--- 413
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAaLLPALEALKRGkgGRVLVLVPtRELAEQWAEELKKLGPSLglk 84

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928     414 --------IQSSEINLVMNGKCGlngmINIISYDLVTK--KKDQILQKNFKVVIADECHYIKqfNSQRSKSTAEVLKR-- 481
Cdd:smart00487   85 vvglyggdSKREQLRKLESGKTD----ILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLL--DGGFGDQLEKLLKLlp 158

                           170       180       190
                    ....*....|....*....|....*....|..
gi 66812928     482 -SKRCILLSGTPalSRPMELFIQISCINPYFM 512
Cdd:smart00487  159 kNVQLLLLSATP--PEEIENLLELFLNDPVFI 188
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 345-492 7.00e-17

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: 80.06  E-value: 7.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGRC---LIADDMGLGKTIQGIS--IAYHYKEEW--PLLIIAPSSLRLVWADQIEKFFP------ 411
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRvggILGDEMGLGKTIQIIAflAALHHSKLGlgPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 -----------NKIQSSEINLVMNGKCGLNGMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlk 480
Cdd:cd18000   81 lhssgsgtgseEKLGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL-- 158

                        170
                 ....*....|..
gi 66812928  481 RSKRCILLSGTP 492
Cdd:cd18000  159 RTPHRLILSGTP 170
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 345-553 1.19e-16

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: 79.79  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEK---GGRCLIADDMGLGKTIQGISI----AYHYKEEWPLLIIAPSSLRLVWADQIEKFFPN----- 412
Cdd:cd18006    1 LRPYQLEGVNWLLQCraeQHGCILGDEMGLGKTCQTISLlwylAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDlsvit 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  413 --KIQSSEINLVMNGKCGLNGMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRSKRCILLSG 490
Cdd:cd18006   81 ymGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEF--SVDFRLLLTG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66812928  491 TPALSRPMELFIQISCINPYFMQwRDYAFRYCAAFQEkfcfNTSGCSNMKELNLYLNTFMIRR 553
Cdd:cd18006  159 TPIQNSLQELYALLSFIEPNVFP-KDKLDDFIKAYSE----TDDESETVEELHLLLQPFLLRR 216
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 344-555 1.26e-16

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: 80.06  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIEFGI---EKGGRCLIADDMGLGKTIQGIS-IAY--HYKE-EWPLLIIAPSSLRLVWADQIEKFFP----- 411
Cdd:cd17997    3 TMRDYQIRGLNWLIslfENGINGILADEMGLGKTLQTISlLGYlkHYKNiNGPHLIIVPKSTLDNWMREFKRWCPslrvv 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 ----NKIQSSEI--NLVMNGK---CglngminIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRS 482
Cdd:cd17997   83 vligDKEERADIirDVLLPGKfdvC-------ITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLF--NS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66812928  483 KRCILLSGTPALSRPMELFIQISCINPYFmqwrdyaFRYCAAFQEKFCFNTSGCSNMK---ELNLYLNTFMIRRLK 555
Cdd:cd17997  154 RNRLLLTGTPLQNNLHELWALLNFLLPDV-------FTSSEDFDEWFNVNNCDDDNQEvvqRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 344-555 1.78e-16

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: 79.74  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIEFGI---EKGGRCLIADDMGLGKTIQGISIAYHYKEE--W-PLLIIAPSSLRLVWADQIEKFFPN----- 412
Cdd:cd18009    3 VMRPYQLEGMEWLRmlwENGINGILADEMGLGKTIQTIALLAHLRERgvWgPFLVIAPLSTLPNWVNEFARFTPSvpvll 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  413 -------------KIQSSEINLVMNGkcglngmINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKStaevL 479
Cdd:cd18009   83 yhgtkeererlrkKIMKREGTLQDFP-------VVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQE----L 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  480 K--RSKRCILLSGTPALSRPMELFIQISCINP-------YFMQWRDYAFRYCAAFQEKFCFNTSGCSNMKELNLYLNTFM 550
Cdd:cd18009  152 KtfNSDNRLLLTGTPLQNNLSELWSLLNFLLPdvfddlsSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFL 231


                 ....*
gi 66812928  551 IRRLK 555
Cdd:cd18009  232 LRRLK 236
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 345-553 5.40e-16

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: 78.48  E-value: 5.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGrcLIADDMGLGKTIQGIS-----------IAYHYKEEWPL----------LIIAPSSLRLVWA 403
Cdd:cd18008    1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALAlilatrpqdpkIPEELEENSSDpkklylskttLIVVPLSLLSQWK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  404 DQIEKFF----------------PNKIQSSEINLVmngkcglngminIISYDLVT----------------KKKDQILQK 451
Cdd:cd18008   79 DEIEKHTkpgslkvyvyhgskriKSIEELSDYDIV------------ITTYGTLAsefpknkkgggrdskeKEASPLHRI 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  452 NFKVVIADECHYIKQFNSQRSKSTAEVlkRSKRCILLSGTPALSR-----PMELFIQISCINPYFMQWRDYAFRycaafq 526
Cdd:cd18008  147 RWYRVILDEAHNIKNRSTKTSRAVCAL--KAERRWCLTGTPIQNSlddlySLLRFLRVEPFGDYPWFNSDISKP------ 218

                        250       260
                 ....*....|....*....|....*..
gi 66812928  527 ekfcFNTSGCSNMKELNLYLNTFMIRR 553
Cdd:cd18008  219 ----FSKNDRKALERLQALLKPILLRR 241
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 345-500 8.15e-16

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: 76.66  E-value: 8.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGI---EKGGRCLIADDMGLGKTIQGISIAYHYKEE---WPLLIIAPSSLRLVWADQIEKFFPN-KI--- 414
Cdd:cd17998    1 LKDYQLIGLNWLNllyQKKLSGILADEMGLGKTIQVIAFLAYLKEIgipGPHLVVVPSSTLDNWLREFKRWCPSlKVepy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  415 ---QSSEINLVMNGKCGLNGmINII--SYDLVTKKKD--QILQK-NFKVVIADECHYIKQFNSQRSKSTAEVLKRSKrcI 486
Cdd:cd17998   81 ygsQEERKHLRYDILKGLED-FDVIvtTYNLATSNPDdrSFFKRlKLNYVVYDEGHMLKNMTSERYRHLMTINANFR--L 157

                        170
                 ....*....|....
gi 66812928  487 LLSGTPALSRPMEL 500
Cdd:cd17998  158 LLTGTPLQNNLLEL 171
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 345-509 1.23e-15

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: 77.80  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF--GIEKGGR-CLIADDMGLGKTIQGISI---AYHYKEEW---------------------PLLIIAPSS 397
Cdd:cd18005    1 LRDYQREGVEFmyDLYKNGRgGILGDDMGLGKTVQVIAFlaaVLGKTGTRrdrennrprfkkkppassakkPVLIVAPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  398 LRLVWADQIEK---FFPNKIQSSEINLVMNGKCGLNGM-INIISYDLVTKKKDQILQKNFKVVIADECHYIKqfnSQRSK 473
Cdd:cd18005   81 VLYNWKDELDTwghFEVGVYHGSRKDDELEGRLKAGRLeVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIK---NPKSK 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 66812928  474 STAEVLK-RSKRCILLSGTPALSRPMELFIQISCINP 509
Cdd:cd18005  158 LTQAMKElKCKVRIGLTGTLLQNNMKELWCLLDWAVP 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 628-748 2.98e-15

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: 72.63  E-value: 2.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    628 KLTAVTQFLKEKlvdapIDQKFLIFAHHKEVINgiVHMLGKikvdKKKLEFIKIDGSTPAQNRNDYVNDFqNDPNCRVaV 707
Cdd:pfam00271    2 KLEALLELLKKE-----RGGKVLIFSQTKKTLE--AELLLE----KEGIKVARLHGDLSQEEREEILEDF-RKGKIDV-L 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 66812928    708 LSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYG 748
Cdd:pfam00271   69 VATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 363-553 5.63e-15

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: 75.36  E-value: 5.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  363 CLIADDMGLGKTIQGISIAYH----YKEEWPLLIIAPSSLRLVWADQIEKFFP-------------NKIQSSEINLVMNG 425
Cdd:cd17995   22 CILADEMGLGKTIQSIAFLEHlyqvEGIRGPFLVIAPLSTIPNWQREFETWTDmnvvvyhgsgesrQIIQQYEMYFKDAQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  426 KCGLNGM----INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQrsksTAEVLKRSK--RCILLSGTPALSRPME 499
Cdd:cd17995  102 GRKKKGVykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSK----LLQGLKKLTleHKLLLTGTPLQNNTEE 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66812928  500 LFIQISCINPyfmqwrdYAFRYCAAFQEKFCFNTSGcSNMKELNLYLNTFMIRR 553
Cdd:cd17995  178 LWSLLNFLEP-------EKFPSSEEFLEEFGDLKTA-EQVEKLQALLKPYMLRR 223
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 345-509 5.41e-14

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: 72.57  E-value: 5.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF------GIEKGGR--CLIADDMGLGKTIQGISIAYHYKEEWP---------LLIIAPSSLRLVWADQIE 407
Cdd:cd18066    1 LRPHQREGIEFlyecvmGMRVNERfgAILADEMGLGKTLQCISLIWTLLRQGPyggkpvikrALIVTPGSLVKNWKKEFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  408 KFfpnkIQSSEINL-VMNGKCGLNGMIN-------IISYDLVTKKKDQILQKNFKVVIADECHYIKqfNSQRSKSTAEVL 479
Cdd:cd18066   81 KW----LGSERIKVfTVDQDHKVEEFIAsplysvlIISYEMLLRSLDQISKLNFDLVICDEGHRLK--NTSIKTTTALTS 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 66812928  480 KRSKRCILLSGTPALSRPMELFIQISCINP 509
Cdd:cd18066  155 LSCERRIILTGTPIQNDLQEFFALIDFVNP 184
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 348-553 2.43e-13

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: 70.61  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  348 FQIKGIEFGI---EKGGRCLIADDMGLGKTIQGISIAYHYKEE---W-PLLIIAPSSLRLVWADQIEKFFP--------- 411
Cdd:cd18002    4 YQLKGLNWLAnlyEQGINGILADEMGLGKTVQSIAVLAHLAEEhniWgPFLVIAPASTLHNWQQEISRFVPqfkvlpywg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 NKIQSSEINLVMNGKcGLNGM-----INIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVLKRSKrcI 486
Cdd:cd18002   84 NPKDRKVLRKFWDRK-NLYTRdapfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNR--L 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66812928  487 LLSGTPALSRPMELFIQISCINPYFMQWRDYAFRYCAAFQEKFCFNTSGCS--NMKELNLYLNTFMIRR 553
Cdd:cd18002  161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNehQLKRLHMILKPFMLRR 229
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 345-553 2.54e-13

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: 70.96  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF------GIEKGGR--CLIADDMGLGKTIQGISIAYHYKEEWP--------LLIIAPSSLRLVWADQIEK 408
Cdd:cd18067    1 LRPHQREGVKFlyrcvtGRRIRGShgCIMADEMGLGKTLQCITLMWTLLRQSPqckpeidkAIVVSPSSLVKNWANELGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  409 FFPNKIQ--------SSEINLVMNGKCGLNGM-----INIISYDLVTKKKDQILQKNFKVVIADECHYIKqfNSQRSKST 475
Cdd:cd18067   81 WLGGRLQplaidggsKKEIDRKLVQWASQQGRrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLK--NSDNQTYQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  476 AEVLKRSKRCILLSGTPALSRPMELFIQISCINPYFMQWRdyafrycAAFQEKFCF--------------NTSGCSNMKE 541
Cdd:cd18067  159 ALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTA-------AEFKKNFELpilkgrdadasekeRQLGEEKLQE 231

                        250
                 ....*....|..
gi 66812928  542 LNLYLNTFMIRR 553
Cdd:cd18067  232 LISIVNRCIIRR 243
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
344-855 2.82e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.91  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIE----FGIEKGGRCLIADDMGLGKTIQGISIAYHYKEEWPLLIIAPS-SLRLVWADQIEKFFPNKIQSSe 418
Cdd:COG1061   80 ELRPYQQEALEallaALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRrELLEQWAEELRRFLGDPLAGG- 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  419 inlvmnGKCGLNGMINIISYD-LVTKKKDQILQKNFKVVIADECHYIkqfnsqRSKSTAEVLKR--SKRCILLSGTPALS 495
Cdd:COG1061  159 ------GKKDSDAPITVATYQsLARRAHLDELGDRFGLVIIDEAHHA------GAPSYRRILEAfpAAYRLGLTATPFRS 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  496 --RPMELFIQISCInpyfmqwrdYAFRYCAAFQEKfcfntsgcsnmkelnlYLNTFMIRRLKDDVMTEL-----PEKRRE 568
Cdd:COG1061  227 dgREILLFLFDGIV---------YEYSLKEAIEDG----------------YLAPPEYYGIRVDLTDERaeydaLSERLR 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  569 RILVKLDKTKLKEVQKTLVEINQHRKVyldpntdmktsfknknsrqglffkllrdtglykltavtqflkeklvdapidqk 648
Cdd:COG1061  282 EALAADAERKDKILRELLREHPDDRKT----------------------------------------------------- 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  649 fLIFAHHKEVINGIVHMLGKIKVDKkklefIKIDGSTPAQNRNDYVNDFQNDPncRVAVLSITAAGTGLTLTAATCVIFA 728
Cdd:COG1061  309 -LVFCSSVDHAEALAELLNEAGIRA-----AVVTGDTPKKEREEILEAFRDGE--LRILVTVDVLNEGVDVPRLDVAILL 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  729 ELSWTPGVLFQAEDRAHRYGQTSSVLVQYLIAlGTVDEMIWSLVESKKTLLGRVLDDEDGQSLNAEDAGQLEHGEQSVDD 808
Cdd:COG1061  381 RPTGSPREFIQRLGRGLRPAPGKEDALVYDFV-GNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKG 459

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 66812928  809 FIDSLIKKVEEQDQIRKKKYDDKQRRKEEKLLKLQLKNGSGGGGGEE 855
Cdd:COG1061  460 ELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAE 506
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 338-566 3.39e-13

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: 70.46  E-value: 3.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  338 FSELPS-----TLLPFQIKGIEFGI---EKGGRCLIADDMGLGKTIQGISI---AYHYKE-EWPLLIIAPSSLRLVWADQ 405
Cdd:cd18064    4 FEDSPSyvkwgKLRDYQVRGLNWLIslyENGINGILADEMGLGKTLQTISLlgyMKHYRNiPGPHMVLVPKSTLHNWMAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  406 IEKFFP---------NKIQSSEI--NLVMNGKCGlngmINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKS 474
Cdd:cd18064   84 FKRWVPtlravcligDKDQRAAFvrDVLLPGEWD----VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  475 TAEvLKRSKRcILLSGTPALSRPMELFIQISCINPYFMQWRDYAFRYcaafqekfcFNTSGCSN----MKELNLYLNTFM 550
Cdd:cd18064  160 VRE-FKTTNR-LLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSW---------FDTNNCLGdqklVERLHMVLRPFL 228

                        250
                 ....*....|....*.
gi 66812928  551 IRRLKDDVMTELPEKR 566
Cdd:cd18064  229 LRRIKADVEKSLPPKK 244
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 344-554 6.02e-13

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: 69.32  E-value: 6.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIEF----------GIekggrclIADDMGLGKTIQGIS-IAYHY---KEEWPLLIIAPSSLRLVWADQIEKF 409
Cdd:cd17996    3 TLKEYQLKGLQWmvslynnnlnGI-------LADEMGLGKTIQTISlITYLMekkKNNGPYLVIVPLSTLSNWVSEFEKW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  410 FP------------------NKIQSSEINLVMNgkcglngminiiSYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQR 471
Cdd:cd17996   76 APsvskivykgtpdvrkklqSQIRAGKFNVLLT------------TYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  472 SkSTAEVLKRSKRCILLSGTPALSRPMELFIQISCINPYFmqwrdyaFRYCAAFQEKFC--FNTSGCSNMKELNLYLNTF 549
Cdd:cd17996  144 T-QTLNTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKI-------FKSCKTFEQWFNtpFANTGEQVKIELNEEETLL 215


                 ....*
gi 66812928  550 MIRRL 554
Cdd:cd17996  216 IIRRL 220
HELICc smart00490
helicase superfamily c-terminal domain;
673-748 6.19e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.93  E-value: 6.19e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66812928     673 KKKLEFIKIDGSTPAQNRNDYVNDFQNDPNcrVAVLSITAAGTGLTLTAATCVIFAELSWTPGVLFQAEDRAHRYG 748
Cdd:smart00490    9 ELGIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 345-492 1.09e-12

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: 68.55  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF--GIEKGGR-CLIADDMGLGKTIQGISI---AYHYKEEWPLLIIAPSSLRLVWADQIEKFFPN------ 412
Cdd:cd18001    1 LYPHQREGVAWlwSLHDGGKgGILADDMGLGKTVQICAFlsgMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGlrvkvf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  413 ---KIQSSEINLvmnGKCGLNGMINIISYDLVTKKKDQI---LQKNFK--VVIADECHYIKQFNSQRSKSTAEVlkRSKR 484
Cdd:cd18001   81 hgtSKKERERNL---ERIQRGGGVLLTTYGMVLSNTEQLsadDHDEFKwdYVILDEGHKIKNSKTKSAKSLREI--PAKN 155


                 ....*...
gi 66812928  485 CILLSGTP 492
Cdd:cd18001  156 RIILTGTP 163
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 360-507 5.08e-11

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: 64.03  E-value: 5.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  360 GGrcLIADDMGLGKTIQGIS-IAYHykeewPLLIIAPSSLRLVWADQIE--------KFF----PNKIQssEINLVMNGK 426
Cdd:cd18071   50 GG--ILADDMGLGKTLTTISlILAN-----FTLIVCPLSVLSNWETQFEehvkpgqlKVYtyhgGERNR--DPKLLSKYD 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  427 CGLNgMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEvLKRSKRCIlLSGTPALSRPMELFIQISC 506
Cdd:cd18071  121 IVLT-TYNTLASDFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLN-LSSERRWV-LTGTPIQNSPKDLGSLLSF 197


                 .
gi 66812928  507 I 507
Cdd:cd18071  198 L 198
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 338-555 6.50e-11

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: 63.50  E-value: 6.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  338 FSELPS-----TLLPFQIKGIEFGI---EKGGRCLIADDMGLGKTIQGISI---AYHYKE-EWPLLIIAPSSLRLVWADQ 405
Cdd:cd18065    4 FEESPSyvkggTLRDYQVRGLNWMIslyENGVNGILADEMGLGKTLQTIALlgyLKHYRNiPGPHMVLVPKSTLHNWMNE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  406 IEKFFPN----------KIQSSEI-NLVMNGKCGlngmINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKS 474
Cdd:cd18065   84 FKRWVPSlravcligdkDARAAFIrDVMMPGEWD----VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  475 TAEvLKRSKRcILLSGTPALSRPMELFIQISCINPYFMQWRDyafRYCAAFQEKFCFNTSGCsnMKELNLYLNTFMIRRL 554
Cdd:cd18065  160 VRE-FKTTNR-LLLTGTPLQNNLHELWALLNFLLPDVFNSAD---DFDSWFDTKNCLGDQKL--VERLHAVLKPFLLRRI 232


                 .
gi 66812928  555 K 555
Cdd:cd18065  233 K 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 344-554 6.90e-11

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: 63.93  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIEFGIEKGGRCL---IADDMGLGKTIQGIS-IAY---HYKEEWPLLIIAPSSLRLVWADQIEKFFPNKIQS 416
Cdd:cd18063   23 TLKHYQLQGLEWMVSLYNNNLngiLADEMGLGKTIQTIAlITYlmeHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  417 S-------EINLVMNGKCGLNGMInIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVLKRSKRcILLS 489
Cdd:cd18063  103 SykgtpamRRSLVPQLRSGKFNVL-LTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRR-ILLT 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66812928  490 GTPALSRPMELFIQISCINPYFmqwrdyaFRYCAAFQEKFCFNTSGCSNMKELNLYLNTFMIRRL 554
Cdd:cd18063  181 GTPLQNKLPELWALLNFLLPTI-------FKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRL 238
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 345-554 8.90e-11

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: 63.52  E-value: 8.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGRCL---IADDMGLGKTIQGIS-IAY---HYKEEWPLLIIAPSSLRLVWADQIEKFFPNKIQSS 417
Cdd:cd18062   24 LKQYQIKGLEWLVSLYNNNLngiLADEMGLGKTIQTIAlITYlmeHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  418 EINLVMNGKCGL----NGMINII--SYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVLKRSKRcILLSGT 491
Cdd:cd18062  104 YKGSPAARRAFVpqlrSGKFNVLltTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRR-LLLTGT 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66812928  492 PALSRPMELFIQISCINPYFmqwrdyaFRYCAAFQEKFCFNTSGCSNMKELNLYLNTFMIRRL 554
Cdd:cd18062  183 PLQNKLPELWALLNFLLPTI-------FKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRL 238
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 359-517 3.90e-10

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: 61.22  E-value: 3.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  359 KGGRCLIADDMGLGKTIQGIS-IAYHYKEEW---PLLIIAPSSLRLVWADQIEKFFP--------------NKIQSSEIN 420
Cdd:cd18053   38 KGNSCILADEMGLGKTIQTISfLNYLFHEHQlygPFLLVVPLSTLTSWQREIQTWAPqmnavvylgdinsrNMIRTHEWM 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  421 LVMNGKCGLNgmINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRSKRCILLSGTPALSRPMEL 500
Cdd:cd18053  118 HPQTKRLKFN--ILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDF--KSNHRLLITGTPLQNSLKEL 193

                        170
                 ....*....|....*...
gi 66812928  501 FIQISCINP-YFMQWRDY 517
Cdd:cd18053  194 WSLLHFIMPeKFSSWEDF 211
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 344-553 4.54e-10

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: 60.83  E-value: 4.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  344 TLLPFQIKGIEFGIE---KGGRCLIADDMGLGKTIQGIS-IAYHYKEEW---PLLIIAPSSLRLVWADQIEKFFP----- 411
Cdd:cd17993    1 ELRDYQLTGLNWLAHswcKGNNGILADEMGLGKTVQTISfLSYLFHSQQqygPFLVVVPLSTMPAWQREFAKWAPdmnvi 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 ---------NKIQSSEINLVMNGKCGLNGMINiiSYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRS 482
Cdd:cd17993   81 vylgdiksrDTIREYEFYFSQTKKLKFNVLLT--TYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF--KT 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66812928  483 KRCILLSGTPALSRPMELFIQISCINPY-FMQWRDYAFRYcAAFQEKfcfntsgcsNMKELNLYLNTFMIRR 553
Cdd:cd17993  157 NNRLLITGTPLQNSLKELWALLHFLMPGkFDIWEEFEEEH-DEEQEK---------GIADLHKELEPFILRR 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 345-517 7.44e-10

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: 60.40  E-value: 7.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGRC---LIADDMGLGKTIQGIS-IAYHYKEEW---PLLIIAPSSLRLVWADQIEKFFP------ 411
Cdd:cd18054   21 LRDYQLEGLNWLAHSWCKNnsvILADEMGLGKTIQTISfLSYLFHQHQlygPFLLVVPLSTLTSWQREFEIWAPeinvvv 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 --------NKIQSSEINLVMNGKCGLNGMINiiSYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVlkRSK 483
Cdd:cd18054  101 yigdlmsrNTIREYEWIHSQTKRLKFNALIT--TYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDF--KSN 176

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 66812928  484 RCILLSGTPALSRPMELFIQISCINP-YFMQWRDY 517
Cdd:cd18054  177 HRLLITGTPLQNSLKELWSLLHFIMPeKFEFWEDF 211
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 345-553 7.69e-10

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: 59.38  E-value: 7.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGI---EFGIEKGGRCLIADDMGLGKTIQGISIAYH-YKE---EWPLLIIAPSSLRLVWADQIEKFFPnkiqss 417
Cdd:cd17994    1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVFLYSlYKEghsKGPFLVSAPLSTIINWEREFEMWAP------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  418 eiNLVMNGKCGLNGMINiiSYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVLKRSKrcILLSGTPALSRP 497
Cdd:cd17994   75 --DFYVVTYVGDHVLLT--SYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYK--LLLTGTPLQNNL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 66812928  498 MELFIQISCINP-YFMQWRdyafrycaAFQEKFCfNTSGCSNMKELNLYLNTFMIRR 553
Cdd:cd17994  149 EELFHLLNFLTPeRFNNLQ--------GFLEEFA-DISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 345-553 3.56e-09

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: 58.54  E-value: 3.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGI---EFGIEKGGRCLIADDMGLGKTIQGISIAYH-YKE---EWPLLIIAPSSLRLVWADQIEKFFP------ 411
Cdd:cd18057    1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTIVFLYSlYKEghsKGPYLVSAPLSTIINWEREFEMWAPdfyvvt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 --------------------NKIQSSEINLVMNGKCGLNGMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQR 471
Cdd:cd18057   81 ytgdkesrsvirenefsfedNAIRSGKKVFRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  472 SKstaeVLKRSK--RCILLSGTPALSRPMELFIQISCINPyfmqwrdYAFRYCAAFQEKFCfNTSGCSNMKELNLYLNTF 549
Cdd:cd18057  161 FR----VLNSYKidYKLLLTGTPLQNNLEELFHLLNFLTP-------ERFNNLEGFLEEFA-DISKEDQIKKLHDLLGPH 228


                 ....
gi 66812928  550 MIRR 553
Cdd:cd18057  229 MLRR 232
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 345-492 1.04e-08

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 55.00  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIE--FGIEKGGRCLIADDMGLGKTIQGISIAYHYKEEwPLLIIAPS-SLRLVWADQIEKFFPNK---IQSSE 418
Cdd:cd17926    1 LRPYQEEALEawLAHKNNRRGILVLPTGSGKTLTALALIAYLKEL-RTLIVVPTdALLDQWKERFEDFLGDSsigLIGGG 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66812928  419 INlvmngKCGLNGMINIISYDLVTK--KKDQILQKNFKVVIADECHYIKqfnsqrSKSTAEVLKRSKR-CIL-LSGTP 492
Cdd:cd17926   80 KK-----KDFDDANVVVATYQSLSNlaEEEKDLFDQFGLLIVDEAHHLP------AKTFSEILKELNAkYRLgLTATP 146
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 345-534 2.38e-08

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: 56.05  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIE------------KGGRCLIADDMGLGKTIQGISIAY----HYKEE--WPLLIIAPSSLRLVWADQI 406
Cdd:cd18068    1 LKPHQVDGVQFMWDccceslkktkksPGSGCILAHCMGLGKTLQVVTFLHtvllCEKLEnfSRVLVVCPLNTVLNWLNEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  407 EKFF-----PNKIQSSEINLV--------MNGKCGLNGMINIISYDL---VTKKKDQILQKNFK-------------VVI 457
Cdd:cd18068   81 EKWQeglkdEEKIEVNELATYkrpqersyKLQRWQEEGGVMIIGYDMyriLAQERNVKSREKLKeifnkalvdpgpdFVV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66812928  458 ADECHYIKqfNSQRSKSTAEVLKRSKRCILLSGTPALSRPMELFIQISCINPYFM-QWRDYAFRYCAAFQEKFCFNTS 534
Cdd:cd18068  161 CDEGHILK--NEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLgTIKEFRNRFVNPIQNGQCADST 236
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 345-553 6.82e-08

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: 54.69  E-value: 6.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGI---EFGIEKGGRCLIADDMGLGKTIQGISIAYH-YKE---EWPLLIIAPSSLRLVWADQIEKFFP------ 411
Cdd:cd18056    1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTAVFLYSlYKEghsKGPFLVSAPLSTIINWEREFEMWAPdmyvvt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 --------------------NKIQSSEINLVMNGKCGLNGMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQR 471
Cdd:cd18056   81 yvgdkdsraiirenefsfedNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  472 SKSTAEVLKRSKrcILLSGTPALSRPMELFIQISCINPyfmqwrdYAFRYCAAFQEKFCfNTSGCSNMKELNLYLNTFMI 551
Cdd:cd18056  161 FRVLNGYSLQHK--LLLTGTPLQNNLEELFHLLNFLTP-------ERFHNLEGFLEEFA-DIAKEDQIKKLHDMLGPHML 230


                 ..
gi 66812928  552 RR 553
Cdd:cd18056  231 RR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 345-509 7.36e-08

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: 54.29  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISI---AYHYKEEWPLLIIAPSSLRLVWadqiEKFFPNKIQSSE 418
Cdd:cd18060    1 LREYQLEGVNwllFNWYNRQNCILADEMGLGKTIQSIAFlqeVYNVGIHGPFLVIAPLSTITNW----EREFNTWTEMNT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  419 InlVMNGKCGLNGMIN-----------------------IISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKST 475
Cdd:cd18060   77 I--VYHGSLASRQMIQqyemyckdsrgrlipgaykfdalITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSL 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 66812928  476 AEVLKRSKrcILLSGTPALSRPMELFIQISCINP 509
Cdd:cd18060  155 KHMDLEHK--VLLTGTPLQNTVEELFSLLHFLEP 186
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 345-515 1.34e-07

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: 53.67  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEF----GIEKGGR--------CLIADDMGLGKTIQGISIAYHYKEEWPL---LIIAPSSLRLVWADQIEKF 409
Cdd:cd18069    1 LKPHQIGGIRFlydnIIESLERykgssgfgCILAHSMGLGKTLQVISFLDVLLRHTGAktvLAIVPVNTLQNWLSEFNKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  410 FPN-------KIQSSEINLVMNGKCGLNGMINIISyDLVTKKKDQIL-QKNFK------VVIADECHYIKqfNSQRSKST 475
Cdd:cd18069   81 LPPpealpnvRPRPFKVFILNDEHKTTAARAKVIE-DWVKDGGVLLMgYEMFRlrpgpdVVICDEGHRIK--NCHASTSQ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 66812928  476 AEVLKRSKRCILLSGTPALSRPMELFIQISCINPYFMQWR 515
Cdd:cd18069  158 ALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTR 197
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 348-553 2.21e-07

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: 53.09  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  348 FQIKGI---EFGIEKGGRCLIADDMGLGKTIQGISIAYH-YKE---EWPLLIIAPSSLRLVWADQIEKFFP--------- 411
Cdd:cd18055    4 YQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVFLYSlYKEghtKGPFLVSAPLSTIINWEREFQMWAPdfyvvtytg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 -----------------NKIQSSEINLVMNGKCGLNGMINIISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKS 474
Cdd:cd18055   84 dkdsraiirenefsfddNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRV 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66812928  475 TAEVLKRSKrcILLSGTPALSRPMELFIQISCINPyfmqwrdYAFRYCAAFQEKFCfNTSGCSNMKELNLYLNTFMIRR 553
Cdd:cd18055  164 LNGYKIDHK--LLLTGTPLQNNLEELFHLLNFLTP-------ERFNNLEGFLEEFA-DISKEDQIKKLHDLLGPHMLRR 232
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 345-411 1.69e-06

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: 50.81  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIEFGIEKGGrcLIADDMGLGKTIQGIS-IAYHYKEEWPL----------------------------LIIAP 395
Cdd:cd18070    1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLAlILLHPRPDNDLdaadddsdemvccpdclvaetpvsskatLIVCP 78

                         90
                 ....*....|....*.
gi 66812928  396 SSLRLVWADQIEKFFP 411
Cdd:cd18070   79 SAILAQWLDEINRHVP 94
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 345-553 1.92e-06

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: 50.04  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISIAYH---YKEEWPLLIIAPSSLRLVW---------------- 402
Cdd:cd18058    1 LREYQLEGMNwllFNWYNRKNCILADEMGLGKTIQSITFLSEiflMGIRGPFLIIAPLSTITNWerefrtwtemnaivyh 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  403 ADQIEKFFPNKIQ---SSEINLVMNGKCGLNGMINiiSYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVL 479
Cdd:cd18058   81 GSQISRQMIQQYEmyyRDEQGNPLSGIFKFQVVIT--TFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66812928  480 KRSKrcILLSGTPALSRPMELFIQISCINPyfmqwrdYAFRYCAAFQEKFCfNTSGCSNMKELNLYLNTFMIRR 553
Cdd:cd18058  159 LEHK--VLLTGTPLQNSVEELFSLLNFLEP-------SQFPSETTFLEEFG-DLKTEEQVKKLQSILKPMMLRR 222
ResIII pfam04851
Type III restriction enzyme, res subunit;
370-492 9.62e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.90  E-value: 9.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928    370 GLGKTIQGISIAYHYKEEWPL---LIIAPS-SLRLVWADQIEKFFPNKIQSSEInlvMNGKC----GLNGMINIISYD-- 439
Cdd:pfam04851   33 GSGKTLTAAKLIARLFKKGPIkkvLFLVPRkDLLEQALEEFKKFLPNYVEIGEI---ISGDKkdesVDDNKIVVTTIQsl 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 66812928    440 --LVTKKKDQILQKNFKVVIADECHYIkQFNSQRskstaEVLKRSKRCILL--SGTP 492
Cdd:pfam04851  110 ykALELASLELLPDFFDVIIIDEAHRS-GASSYR-----NILEYFKPAFLLglTATP 160
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 345-509 8.49e-05

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: 45.02  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISIAYHYKEE---WPLLIIAPSSLRLVWADQIEKFFP------- 411
Cdd:cd18059    1 LREYQLEGVNwllFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKgihGPFLVIAPLSTIPNWEREFRTWTElnvvvyh 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  412 ------NKIQSSEINL------VMNGKCGLNGMINiiSYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKSTAEVL 479
Cdd:cd18059   81 gsqasrRTIQLYEMYFkdpqgrVIKGSYKFHAIIT--TFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 66812928  480 KRSKrcILLSGTPALSRPMELFIQISCINP 509
Cdd:cd18059  159 LEHK--VLLTGTPLQNTVEELFSLLHFLEP 186
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
 370-463 2.09e-04

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 42.93  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  370 GLGKTIQGISIAYHYKEEWP---LLIIAPsslRLVWADQ-IEKFFPNKIQSSEINLVMNGKCGLNGMINIISYD-LVTKK 444
Cdd:cd18032   30 GTGKTYTAAFLIKRLLEANRkkrILFLAH---REELLEQaERSFKEVLPDGSFGNLKGGKKKPDDARVVFATVQtLNKRK 106

                         90       100
                 ....*....|....*....|
gi 66812928  445 KDQILQKN-FKVVIADECHY 463
Cdd:cd18032  107 RLEKFPPDyFDLIIIDEAHH 126
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 345-509 5.43e-04

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: 42.69  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  345 LLPFQIKGIE---FGIEKGGRCLIADDMGLGKTIQGISIAYHYKE---EWPLLIIAPSSLRLVWADQIEKFfpnkiqsSE 418
Cdd:cd18061    1 LREYQLEGLNwllFNWYNRRNCILADEMGLGKTIQSITFLYEILLtgiRGPFLIIAPLSTIANWEREFRTW-------TD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  419 INLVM-NGKCGLNGMIN-----------------------IISYDLVTKKKDQILQKNFKVVIADECHYIKQFNSQRSKS 474
Cdd:cd18061   74 LNVVVyHGSLISRQMIQqyemyfrdsqgriirgayrfqaiITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEG 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 66812928  475 TAevLKRSKRCILLSGTPALSRPMELFIQISCINP 509
Cdd:cd18061  154 LK--LMNLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 360-491 5.92e-04

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: 41.23  E-value: 5.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66812928  360 GGRCLIADDMGLGKTIQGISIAYHYKEEWPL--LIIAP-SSLRLVWADQIEKFFPNKIQ------SSEINLVMNGKCGLN 430
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKKGKkvLVLVPtKALALQTAERLRELFGPGIRvavlvgGSSAEEREKNKLGDA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66812928  431 GMInIISYDLVTKKK---DQILQKNFKVVIADECHYI----KQFNSQRSKSTAEVLKRSKRcILLSGT 491
Cdd:cd00046   81 DII-IATPDMLLNLLlreDRLFLKDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQV-ILLSAT 146
 
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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