NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1944867412|ref|XP_027317207|]
View 

LOW QUALITY PROTEIN: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 [Anas platyrhynchos]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
465-674 2.14e-122

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: 371.15  E-value: 2.14e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGRLLLADDMGLGKTIQAICVAAYYRKEWPLLVVTPSSVRFTWAEAFHRWLPSLRPGSTNVIVTG 544
Cdd:cd18010     1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 545 KDNL--TGSLINIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLLKAARRVILLSGTPAMSRPMELYT 621
Cdd:cd18010    81 KDGLrdGDAKVVIVSYDLLRRLEKQLLArKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELFT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1944867412 622 QIAAVQPDFFPQFHTFGLRYCDAKQMPWGWDYSGSSNLAELKILLEESIMIRR 674
Cdd:cd18010   161 QLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
737-862 1.35e-48

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: 168.81  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 737 AKIHSVVEYILELLESGkDKFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVAVLSLTAA 816
Cdd:cd18793    11 GKLEALLELLEELREPG-EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1944867412 817 NMGLTLSAADLVVFAELFWNPGVLIQAEDRAHRIGQTSSVNVHYVV 862
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
268-322 1.09e-27

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


:

Pssm-ID: 462166  Cd Length: 55  Bit Score: 106.10  E-value: 1.09e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1944867412 268 FLVEIGYNAELIAVFKKIPSKSYDPTMKKWNFSLEDYISFMEAANRLSSVILEPL 322
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
373-427 7.20e-26

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


:

Pssm-ID: 462166  Cd Length: 55  Bit Score: 100.71  E-value: 7.20e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1944867412 373 FEVDIGYSAEVIGVFKQMNSRNYDAKTRKWNFLLEDYPKLVKMFQSLASVQVEPL 427
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
465-674 2.14e-122

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: 371.15  E-value: 2.14e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGRLLLADDMGLGKTIQAICVAAYYRKEWPLLVVTPSSVRFTWAEAFHRWLPSLRPGSTNVIVTG 544
Cdd:cd18010     1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 545 KDNL--TGSLINIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLLKAARRVILLSGTPAMSRPMELYT 621
Cdd:cd18010    81 KDGLrdGDAKVVIVSYDLLRRLEKQLLArKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELFT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1944867412 622 QIAAVQPDFFPQFHTFGLRYCDAKQMPWGWDYSGSSNLAELKILLEESIMIRR 674
Cdd:cd18010   161 QLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
463-880 2.97e-95

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 316.01  E-value: 2.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 463 TSLMPFQREGVNFAIFR---NGRLLLADDMGLGKTIQAICVAAYYRKE---WPLLVVTPSSVRFTWAEAFHRWLPSLRPg 536
Cdd:COG0553   240 ATLRPYQLEGAAWLLFLrrlGLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAPGLRV- 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 537 stnVIVTGKDN-------LTGSLINIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLlkAARRVILLS 608
Cdd:COG0553   319 ---LVLDGTRErakganpFEDADLVITSYGLLRRDIELLAAvDWDLVILDEAQHIKNPATKRAKAVRAL--KARHRLALT 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 609 GTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAKQmpwgwdYSGSSNLAELKILLEEsIMIRRLKSDVLSQLPAKQR 688
Cdd:COG0553   394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE------KGDEEALERLRRLLRP-FLLRRTKEDVLKDLPEKTE 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 689 KMVVVSPEGINAKT-KAALAVEAKKMAKGYGNKQQEK--EALL----------LFYNRTAE-----AKIHSVVEYILELL 750
Cdd:COG0553   467 ETLYVELTPEQRALyEAVLEYLRRELEGAEGIRRRGLilAALTrlrqicshpaLLLEEGAElsgrsAKLEALLELLEELL 546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 751 ESGkDKFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVAVLSLTAANMGLTLSAADLVVF 830
Cdd:COG0553   547 AEG-EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIH 625
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1944867412 831 AELFWNPGVLIQAEDRAHRIGQTSSVNVHYVVAKGTADDFLWPMIQEKIK 880
Cdd:COG0553   626 YDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
737-862 1.35e-48

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: 168.81  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 737 AKIHSVVEYILELLESGkDKFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVAVLSLTAA 816
Cdd:cd18793    11 GKLEALLELLEELREPG-EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1944867412 817 NMGLTLSAADLVVFAELFWNPGVLIQAEDRAHRIGQTSSVNVHYVV 862
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
454-858 6.02e-33

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 138.01  E-value: 6.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  454 LSVVDSKIVTSLMPFQREGVNFAI--FRNG-RLLLADDMGLGKTIQAICVAAY---YRK-EWPLLVVTPSSVRFTWAEAF 526
Cdd:PLN03142   159 LLVQPSCIKGKMRDYQLAGLNWLIrlYENGiNGILADEMGLGKTLQTISLLGYlheYRGiTGPHMVVAPKSTLGNWMNEI 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  527 HRWLPSLRP----GSTNVIVTGKDNL--TGSL-INIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNvKTARCRAAMPLL 598
Cdd:PLN03142   239 RRFCPVLRAvkfhGNPEERAHQREELlvAGKFdVCVTSFEMAIKEKTALKRfSWRYIIIDEAHRIKN-ENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  599 KAARRvILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGlrycdakqmPWgWDYSGSSNLAEL-----KILleESIMIR 673
Cdd:PLN03142   318 STNYR-LLITGTPLQNNLHELWALLNFLLPEIFSSAETFD---------EW-FQISGENDQQEVvqqlhKVL--RPFLLR 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  674 RLKSDVLSQLPAKQrkmvvvspEGInaktkaaLAVEAKKMAKGYGNK--QQEKEALllfyNRTAE-AKIHSVV------- 743
Cdd:PLN03142   385 RLKSDVEKGLPPKK--------ETI-------LKVGMSQMQKQYYKAllQKDLDVV----NAGGErKRLLNIAmqlrkcc 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  744 ------------------EYILEllESGK----DKF-----------LVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSS 790
Cdd:PLN03142   446 nhpylfqgaepgppyttgEHLVE--NSGKmvllDKLlpklkerdsrvLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGG 523
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  791 AERQSLCQKFQL--SEKqAVAVLSLTAANMGLTLSAADLVVFAELFWNPGVLIQAEDRAHRIGQTSSVNV 858
Cdd:PLN03142   524 EDRDASIDAFNKpgSEK-FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQV 592
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
268-322 1.09e-27

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 106.10  E-value: 1.09e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1944867412 268 FLVEIGYNAELIAVFKKIPSKSYDPTMKKWNFSLEDYISFMEAANRLSSVILEPL 322
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
373-427 7.20e-26

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 100.71  E-value: 7.20e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1944867412 373 FEVDIGYSAEVIGVFKQMNSRNYDAKTRKWNFLLEDYPKLVKMFQSLASVQVEPL 427
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
469-691 1.13e-25

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: 108.15  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 469 QREGVNFAI------FRNGrlLLADDMGLGKTIQAICVAAY---YRKEW--PLLVVTPSSVRFTWAEAFHRWlpsLRPGS 537
Cdd:pfam00176   2 QIEGVNWMLslennlGRGG--ILADEMGLGKTLQTISLLLYlkhVDKNWggPTLIVVPLSLLHNWMNEFERW---VSPPA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 TNVIVTGKDN------------LTGSLINIISFDLLSKMDKQLKNT-FQVVIIDESHYLKNVKtARCRAAMPLLKAARRv 604
Cdd:pfam00176  77 LRVVVLHGNKrpqerwkndpnfLADFDVVITTYETLRKHKELLKKVhWHRIVLDEGHRLKNSK-SKLSKALKSLKTRNR- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 605 ILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAKQMPWGwdYSGSSNLAELKilleESIMIRRLKSDVLSQLP 684
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGG--KKGVSRLHKLL----KPFLLRRTKKDVEKSLP 228

                  ....*..
gi 1944867412 685 AKQRKMV 691
Cdd:pfam00176 229 PKVEYIL 235
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
741-851 9.62e-20

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: 85.34  E-value: 9.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 741 SVVEYILELLESGKD-KFLVFAHHKIMLDAivEEL-EKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVavLSLTAANM 818
Cdd:pfam00271   1 EKLEALLELLKKERGgKVLIFSQTKKTLEA--ELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVL--VATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1944867412 819 GLTLSAADLVVFAELFWNPGVLIQAEDRAHRIG 851
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
463-611 6.68e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 86.01  E-value: 6.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  463 TSLMPFQREGVNFAIFRNGRLLLADDMGLGKTIQAICVAAYYRKE---WPLLVVTP-SSVRFTWAEAFHRWLPSLRPGST 538
Cdd:smart00487   7 EPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRgkgGRVLVLVPtRELAEQWAEELKKLGPSLGLKVV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  539 NVIVTGK-----DNLTGSLINII-----SFDLLSKMDKQLKNTFQVVIIDESHYLKNVK-TARCRAAMPLLKAARRVILL 607
Cdd:smart00487  87 GLYGGDSkreqlRKLESGKTDILvttpgRLLDLLENDKLSLSNVDLVILDEAHRLLDGGfGDQLEKLLKLLPKNVQLLLL 166

                   ....
gi 1944867412  608 SGTP 611
Cdd:smart00487 167 SATP 170
HELICc smart00490
helicase superfamily c-terminal domain;
768-851 5.38e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 73.79  E-value: 5.38e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  768 DAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQlsEKQAVAVLSLTAANMGLTLSAADLVVFAELFWNPGVLIQAEDRA 847
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 1944867412  848 HRIG 851
Cdd:smart00490  79 GRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
724-868 1.69e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 52.04  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 724 KEALllfyNRTAEAKI-HSVVEYILELLES-----GKDKFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLC 797
Cdd:COG1111   321 RKAM----RLAEEADIeHPKLSKLREILKEqlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEGDKGLT 396
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944867412 798 QKFQLSEKQA-------VAVlSLTAANMGLTLSAADLVVFAELFWNPgvlIQAEDRAHRIGQTSSVNVHYVVAKGTAD 868
Cdd:COG1111   397 QKEQIEILERfragefnVLV-ATSVAEEGLDIPEVDLVIFYEPVPSE---IRSIQRKGRTGRKREGRVVVLIAKGTRD 470
PRK13766 PRK13766
Hef nuclease; Provisional
738-872 9.65e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.86  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 738 KIHSVVEYILELLESGKD-KFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQlseKQAVA------- 809
Cdd:PRK13766  348 KLEKLREIVKEQLGKNPDsRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQASKDGDKGMSQKEQ---IEILDkfragef 424
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 810 -VL-SLTAANMGLTLSAADLVVFAElfwnPgvlIQAEDRA-HRIGQT---SSVNVHYVVAKGTADD-FLW 872
Cdd:PRK13766  425 nVLvSTSVAEEGLDIPSVDLVIFYE----P---VPSEIRSiQRKGRTgrqEEGRVVVLIAKGTRDEaYYW 487
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
465-674 2.14e-122

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: 371.15  E-value: 2.14e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGRLLLADDMGLGKTIQAICVAAYYRKEWPLLVVTPSSVRFTWAEAFHRWLPSLRPGSTNVIVTG 544
Cdd:cd18010     1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 545 KDNL--TGSLINIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLLKAARRVILLSGTPAMSRPMELYT 621
Cdd:cd18010    81 KDGLrdGDAKVVIVSYDLLRRLEKQLLArKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELFT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1944867412 622 QIAAVQPDFFPQFHTFGLRYCDAKQMPWGWDYSGSSNLAELKILLEESIMIRR 674
Cdd:cd18010   161 QLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
463-880 2.97e-95

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 316.01  E-value: 2.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 463 TSLMPFQREGVNFAIFR---NGRLLLADDMGLGKTIQAICVAAYYRKE---WPLLVVTPSSVRFTWAEAFHRWLPSLRPg 536
Cdd:COG0553   240 ATLRPYQLEGAAWLLFLrrlGLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAPGLRV- 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 537 stnVIVTGKDN-------LTGSLINIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLlkAARRVILLS 608
Cdd:COG0553   319 ---LVLDGTRErakganpFEDADLVITSYGLLRRDIELLAAvDWDLVILDEAQHIKNPATKRAKAVRAL--KARHRLALT 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 609 GTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAKQmpwgwdYSGSSNLAELKILLEEsIMIRRLKSDVLSQLPAKQR 688
Cdd:COG0553   394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE------KGDEEALERLRRLLRP-FLLRRTKEDVLKDLPEKTE 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 689 KMVVVSPEGINAKT-KAALAVEAKKMAKGYGNKQQEK--EALL----------LFYNRTAE-----AKIHSVVEYILELL 750
Cdd:COG0553   467 ETLYVELTPEQRALyEAVLEYLRRELEGAEGIRRRGLilAALTrlrqicshpaLLLEEGAElsgrsAKLEALLELLEELL 546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 751 ESGkDKFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVAVLSLTAANMGLTLSAADLVVF 830
Cdd:COG0553   547 AEG-EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIH 625
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1944867412 831 AELFWNPGVLIQAEDRAHRIGQTSSVNVHYVVAKGTADDFLWPMIQEKIK 880
Cdd:COG0553   626 YDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
737-862 1.35e-48

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: 168.81  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 737 AKIHSVVEYILELLESGkDKFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVAVLSLTAA 816
Cdd:cd18793    11 GKLEALLELLEELREPG-EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1944867412 817 NMGLTLSAADLVVFAELFWNPGVLIQAEDRAHRIGQTSSVNVHYVV 862
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
465-631 3.85e-46

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: 163.51  E-value: 3.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFR---NGRLLLADDMGLGKTIQAICVAAYYRKE----WPLLVVTPSSVRFTWAEAFHRWLPSLR--- 534
Cdd:cd17919     1 LRPYQLEGLNFLLELyenGPGGILADEMGLGKTLQAIAFLAYLLKEgkerGPVLVVCPLSVLENWEREFEKWTPDLRvvv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 535 ---PGSTNVIVTGKDNLTGSLINIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLlkAARRVILLSGT 610
Cdd:cd17919    81 yhgSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKfRWDLVVVDEAHRLKNPKSQLSKALKAL--RAKRRLLLTGT 158
                         170       180
                  ....*....|....*....|.
gi 1944867412 611 PAMSRPMELYTQIAAVQPDFF 631
Cdd:cd17919   159 PLQNNLEELWALLDFLDPPFL 179
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
454-858 6.02e-33

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 138.01  E-value: 6.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  454 LSVVDSKIVTSLMPFQREGVNFAI--FRNG-RLLLADDMGLGKTIQAICVAAY---YRK-EWPLLVVTPSSVRFTWAEAF 526
Cdd:PLN03142   159 LLVQPSCIKGKMRDYQLAGLNWLIrlYENGiNGILADEMGLGKTLQTISLLGYlheYRGiTGPHMVVAPKSTLGNWMNEI 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  527 HRWLPSLRP----GSTNVIVTGKDNL--TGSL-INIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNvKTARCRAAMPLL 598
Cdd:PLN03142   239 RRFCPVLRAvkfhGNPEERAHQREELlvAGKFdVCVTSFEMAIKEKTALKRfSWRYIIIDEAHRIKN-ENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  599 KAARRvILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGlrycdakqmPWgWDYSGSSNLAEL-----KILleESIMIR 673
Cdd:PLN03142   318 STNYR-LLITGTPLQNNLHELWALLNFLLPEIFSSAETFD---------EW-FQISGENDQQEVvqqlhKVL--RPFLLR 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  674 RLKSDVLSQLPAKQrkmvvvspEGInaktkaaLAVEAKKMAKGYGNK--QQEKEALllfyNRTAE-AKIHSVV------- 743
Cdd:PLN03142   385 RLKSDVEKGLPPKK--------ETI-------LKVGMSQMQKQYYKAllQKDLDVV----NAGGErKRLLNIAmqlrkcc 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  744 ------------------EYILEllESGK----DKF-----------LVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSS 790
Cdd:PLN03142   446 nhpylfqgaepgppyttgEHLVE--NSGKmvllDKLlpklkerdsrvLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGG 523
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  791 AERQSLCQKFQL--SEKqAVAVLSLTAANMGLTLSAADLVVFAELFWNPGVLIQAEDRAHRIGQTSSVNV 858
Cdd:PLN03142   524 EDRDASIDAFNKpgSEK-FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQV 592
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
268-322 1.09e-27

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 106.10  E-value: 1.09e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1944867412 268 FLVEIGYNAELIAVFKKIPSKSYDPTMKKWNFSLEDYISFMEAANRLSSVILEPL 322
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
465-676 2.24e-27

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: 111.12  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIF--RNGrL--LLADDMGLGKTIQAICVAAYYRKEW---PLLVVTPSSVRFTWAEAFHRWLPSLRPgs 537
Cdd:cd18012     5 LRPYQKEGFNWLSFlrHYG-LggILADDMGLGKTLQTLALLLSRKEEGrkgPSLVVAPTSLIYNWEEEAAKFAPELKV-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 tnVIVTGKDN-------LTGSLINIISFDLLSK-MDKQLKNTFQVVIIDESHYLKNVKTARCRAAMpLLKAARRvILLSG 609
Cdd:cd18012    82 --LVIHGTKRkreklraLEDYDLVITSYGLLRRdIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVK-ALKADHR-LALTG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1944867412 610 TPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYcdakQMPwGWDYSGSSNLAELKILLEESIMiRRLK 676
Cdd:cd18012   158 TPIENHLGELWSIFDFLNPGLLGSYKRFKKRF----AKP-IEKDGDEEALEELKKLISPFIL-RRLK 218
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
373-427 7.20e-26

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 100.71  E-value: 7.20e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1944867412 373 FEVDIGYSAEVIGVFKQMNSRNYDAKTRKWNFLLEDYPKLVKMFQSLASVQVEPL 427
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
469-691 1.13e-25

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: 108.15  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 469 QREGVNFAI------FRNGrlLLADDMGLGKTIQAICVAAY---YRKEW--PLLVVTPSSVRFTWAEAFHRWlpsLRPGS 537
Cdd:pfam00176   2 QIEGVNWMLslennlGRGG--ILADEMGLGKTLQTISLLLYlkhVDKNWggPTLIVVPLSLLHNWMNEFERW---VSPPA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 TNVIVTGKDN------------LTGSLINIISFDLLSKMDKQLKNT-FQVVIIDESHYLKNVKtARCRAAMPLLKAARRv 604
Cdd:pfam00176  77 LRVVVLHGNKrpqerwkndpnfLADFDVVITTYETLRKHKELLKKVhWHRIVLDEGHRLKNSK-SKLSKALKSLKTRNR- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 605 ILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAKQMPWGwdYSGSSNLAELKilleESIMIRRLKSDVLSQLP 684
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGG--KKGVSRLHKLL----KPFLLRRTKKDVEKSLP 228

                  ....*..
gi 1944867412 685 AKQRKMV 691
Cdd:pfam00176 229 PKVEYIL 235
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
465-631 1.95e-25

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 105.06  E-value: 1.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAI-FRNGRLLLADDMGLGKTIQAICVAAYYRKEW---PLLVVTPSSVRFTW----AEAFHRWLPSLRPG 536
Cdd:cd18011     1 PLPHQIDAVLRALrKPPVRLLLADEVGLGKTIEAGLIIKELLLRGdakRVLILCPASLVEQWqdelQDKFGLPFLILDRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 537 STNVIVTGKDNLTGSL-INIISFDLLSKMDKQ----LKNTFQVVIIDESHYLKN----VKTARCRAAMPLLKAARRVILL 607
Cdd:cd18011    81 TAAQLRRLIGNPFEEFpIVIVSLDLLKRSEERrgllLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKRARHVLLL 160
                         170       180
                  ....*....|....*....|....
gi 1944867412 608 SGTPAMSRPMELYTQIAAVQPDFF 631
Cdd:cd18011   161 TATPHNGKEEDFRALLSLLDPGRF 184
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
465-674 7.39e-24

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: 101.60  E-value: 7.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGrlLLADDMGLGKTIQAICVAA---YYRKEWPL------------------LVVTPSSVRFTWA 523
Cdd:cd18008     1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALALILatrPQDPKIPEeleenssdpkklylskttLIVVPLSLLSQWK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 524 E--AFHRWLPSLRP----GSTN-----------VIVTGKDNLTGSLINIISFDLLSKMDKQLKNTFQV----VIIDESHY 582
Cdd:cd18008    79 DeiEKHTKPGSLKVyvyhGSKRiksieelsdydIVITTYGTLASEFPKNKKGGGRDSKEKEASPLHRIrwyrVILDEAHN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 583 LKNVKTARCRAAMpLLKAARRvILLSGTPAMSRPMELYTQIAavqpdfFPQFHTFGLRYCDAKQMPWGWDYSGSSNLAEL 662
Cdd:cd18008   159 IKNRSTKTSRAVC-ALKAERR-WCLTGTPIQNSLDDLYSLLR------FLRVEPFGDYPWFNSDISKPFSKNDRKALERL 230
                         250
                  ....*....|..
gi 1944867412 663 KILLeESIMIRR 674
Cdd:cd18008   231 QALL-KPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
465-674 4.79e-23

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: 99.28  E-value: 4.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFaIFR--------NGR-LLLADDMGLGKTIQAICVAayyrkeWPLL--------------VVTPSSVRFT 521
Cdd:cd18004     1 LRPHQREGVQF-LYDcltgrrgyGGGgAILADEMGLGKTLQAIALV------WTLLkqgpygkptakkalIVCPSSLVGN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 522 WAEAFHRWLPSLRPG----STNVIVTGKDNLTGSLIN-----IISFDLLSKMDKQLKNT--FQVVIIDESHYLKNVKTaR 590
Cdd:cd18004    74 WKAEFDKWLGLRRIKvvtaDGNAKDVKASLDFFSSAStypvlIISYETLRRHAEKLSKKisIDLLICDEGHRLKNSES-K 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 591 CRAAMPLLKAARRvILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAKQMPWGWDYS------GSSNLAELkI 664
Cdd:cd18004   153 TTKALNSLPCRRR-LLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASeedkelGAERSQEL-S 230
                         250
                  ....*....|
gi 1944867412 665 LLEESIMIRR 674
Cdd:cd18004   231 ELTSRFILRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
465-631 3.00e-22

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: 96.59  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFaIFRN-----------GRLLLADDMGLGKTIQAIC----VAAYYRKEWPLLVVTPSSVRFTWAEAFHRW 529
Cdd:cd18007     1 LKPHQVEGVRF-LWSNlvgtdvgsdegGGCILAHTMGLGKTLQVITflhtYLAAAPRRSRPLVLCPASTLYNWEDEFKKW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 530 LPSLRPGSTNVIV---TGKDNLTGSLIN---------IISFDLLSKM---DKQLKNTFQ------------VVIIDESHY 582
Cdd:cd18007    80 LPPDLRPLLVLVSlsaSKRADARLRKINkwhkeggvlLIGYELFRNLasnATTDPRLKQefiaalldpgpdLLVLDEGHR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1944867412 583 LKNVKTARCRAAMpLLKAARRvILLSGTPAMSRPMELYTQIAAVQPDFF 631
Cdd:cd18007   160 LKNEKSQLSKALS-KVKTKRR-ILLTGTPLQNNLKEYWTMVDFARPKYL 206
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
465-630 1.12e-21

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: 94.73  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGRLL---LADDMGLGKTIQAICVAA---YYRKEW------PLLVVTPSSVRFTWAEAFHRWLP- 531
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLhgiLCDDMGLGKTLQTLCILAsdhHKRANSfnsenlPSLVVCPPTLVGHWVAEIKKYFPn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 532 -SLRP----GSTNVIVTGKDNLTGSLINIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTaRCRAAMPLLKAARRVI 605
Cdd:cd17999    81 aFLKPlayvGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKiEWNYCVLDEGHIIKNSKT-KLSKAVKQLKANHRLI 159
                         170       180
                  ....*....|....*....|....*
gi 1944867412 606 lLSGTPAMSRPMELYTQIAAVQPDF 630
Cdd:cd17999   160 -LSGTPIQNNVLELWSLFDFLMPGY 183
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
465-640 3.38e-21

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: 92.06  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNF-AIFRNGRL--LLADDMGLGKTIQAICVAAYYR---KEWPLLVVTPSSVRFTWAEAFHRWLPSLRP--- 535
Cdd:cd17998     1 LKDYQLIGLNWlNLLYQKKLsgILADEMGLGKTIQVIAFLAYLKeigIPGPHLVVVPSSTLDNWLREFKRWCPSLKVepy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 536 -GST-----------------NVIVTGKdNLTGSliniisfdllSKMDKQL--KNTFQVVIIDESHYLKNVKTARCRAAM 595
Cdd:cd17998    81 yGSQeerkhlrydilkgledfDVIVTTY-NLATS----------NPDDRSFfkRLKLNYVVYDEGHMLKNMTSERYRHLM 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1944867412 596 PLlkAARRVILLSGTPAMSRPMELYTQIAAVQPdffpqfHTFGLR 640
Cdd:cd17998   150 TI--NANFRLLLTGTPLQNNLLELMSLLNFIMP------KPFILR 186
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
741-851 9.62e-20

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: 85.34  E-value: 9.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 741 SVVEYILELLESGKD-KFLVFAHHKIMLDAivEEL-EKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVavLSLTAANM 818
Cdd:pfam00271   1 EKLEALLELLKKERGgKVLIFSQTKKTLEA--ELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVL--VATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1944867412 819 GLTLSAADLVVFAELFWNPGVLIQAEDRAHRIG 851
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
468-631 9.81e-20

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: 88.92  E-value: 9.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 468 FQREGVNFAI--FRNG-RLLLADDMGLGKTIQAICVAAY---YRK-EWPLLVVTPSSVRFTWAEAFHRWLPSLR------ 534
Cdd:cd17997     7 YQIRGLNWLIslFENGiNGILADEMGLGKTLQTISLLGYlkhYKNiNGPHLIIVPKSTLDNWMREFKRWCPSLRvvvlig 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 535 --------------PGSTNVIVTgkdnltgsliniiSFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTArcraampLLK 599
Cdd:cd17997    87 dkeeradiirdvllPGKFDVCIT-------------SYEMVIKEKTVLKKfNWRYIIIDEAHRIKNEKSK-------LSQ 146
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1944867412 600 AARRV-----ILLSGTPAMSRPMELYTQIAAVQPDFF 631
Cdd:cd17997   147 IVRLFnsrnrLLLTGTPLQNNLHELWALLNFLLPDVF 183
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
465-683 3.80e-19

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: 87.83  E-value: 3.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAI--FRNG-RLLLADDMGLGKTIQAICVAAYY--RKEW-PLLVVTPSSVRFTWAEAFHRWLPSL----- 533
Cdd:cd18009     4 MRPYQLEGMEWLRmlWENGiNGILADEMGLGKTIQTIALLAHLreRGVWgPFLVIAPLSTLPNWVNEFARFTPSVpvlly 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 534 ------RPGSTNVIVTGKDNLTGSLINIISFDLLSKMDKQLK-NTFQVVIIDESHYLKNVKtarCRAAMPL--LKAARRv 604
Cdd:cd18009    84 hgtkeeRERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQhYAWKYLIVDEGHRLKNLN---CRLIQELktFNSDNR- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1944867412 605 ILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFglrycdakqMPWgWDYSGSSNLAELKILLEESimirrLKSDVLSQL 683
Cdd:cd18009   160 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSF---------ESW-FDFSSLSDNAADISNLSEE-----REQNIVHML 223
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
465-674 5.39e-19

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: 86.92  E-value: 5.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIF--RNGR-LLLADDMGLGKTIQAIC----VAAYYRKEWPLLVVTPSSVRFTWAEAFHRWLPslrpgs 537
Cdd:cd17995     1 LRDYQLEGVNWLLFnwYNRRnCILADEMGLGKTIQSIAflehLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 TNVIV---TG-------------KDNLTGSLINIISFDLL--------SKMDKQLKNTFQVVIIDESHYLKNvKTARCRA 593
Cdd:cd17995    75 MNVVVyhgSGesrqiiqqyemyfKDAQGRKKKGVYKFDVLittyemviADAEELRKIPWRVVVVDEAHRLKN-RNSKLLQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 594 AMPLLKAARRViLLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAKQmpwgwdysgSSNLAELKILLeESIMIR 673
Cdd:cd17995   154 GLKKLTLEHKL-LLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKT---------AEQVEKLQALL-KPYMLR 222

                  .
gi 1944867412 674 R 674
Cdd:cd17995   223 R 223
DEXDc smart00487
DEAD-like helicases superfamily;
463-611 6.68e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 86.01  E-value: 6.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  463 TSLMPFQREGVNFAIFRNGRLLLADDMGLGKTIQAICVAAYYRKE---WPLLVVTP-SSVRFTWAEAFHRWLPSLRPGST 538
Cdd:smart00487   7 EPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRgkgGRVLVLVPtRELAEQWAEELKKLGPSLGLKVV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  539 NVIVTGK-----DNLTGSLINII-----SFDLLSKMDKQLKNTFQVVIIDESHYLKNVK-TARCRAAMPLLKAARRVILL 607
Cdd:smart00487  87 GLYGGDSkreqlRKLESGKTDILvttpgRLLDLLENDKLSLSNVDLVILDEAHRLLDGGfGDQLEKLLKLLPKNVQLLLL 166

                   ....
gi 1944867412  608 SGTP 611
Cdd:smart00487 167 SATP 170
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
480-637 1.17e-18

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: 86.27  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 480 NGrlLLADDMGLGKTIQAICVAAYY----RKEWPLLVVTPSSVRFTWAEAFHRWLPSLRP----GSTNV-------IVTG 544
Cdd:cd17996    24 NG--ILADEMGLGKTIQTISLITYLmekkKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKivykGTPDVrkklqsqIRAG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 545 KDNLTGSLINIISFD--LLSKMDkqlkntFQVVIIDESHYLKNvktARCRAAMPLLKA--ARRVILLSGTPAMSRPMELY 620
Cdd:cd17996   102 KFNVLLTTYEYIIKDkpLLSKIK------WKYMIIDEGHRMKN---AQSKLTQTLNTYyhARYRLLLTGTPLQNNLPELW 172
                         170
                  ....*....|....*..
gi 1944867412 621 TQIAAVQPDFFPQFHTF 637
Cdd:cd17996   173 ALLNFLLPKIFKSCKTF 189
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
465-637 2.63e-18

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: 85.28  E-value: 2.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNF------AIFRNGRL--LLADDMGLGKTIQAICVAAYYRKEWP---------LLVVTPSSVRFTWAEAFH 527
Cdd:cd18066     1 LRPHQREGIEFlyecvmGMRVNERFgaILADEMGLGKTLQCISLIWTLLRQGPyggkpvikrALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 528 RWLPSLRpgsTNVIVTGKDNLTGSLIN-------IISFDLLSKMDKQLKN-TFQVVIIDESHYLKNvKTARCRAAMPLLK 599
Cdd:cd18066    81 KWLGSER---IKVFTVDQDHKVEEFIAsplysvlIISYEMLLRSLDQISKlNFDLVICDEGHRLKN-TSIKTTTALTSLS 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1944867412 600 AARRVIlLSGTPAMSRPMELYTQIAAVQPDFFPQFHTF 637
Cdd:cd18066   157 CERRII-LTGTPIQNDLQEFFALIDFVNPGILGSLSTY 193
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
465-687 1.07e-17

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: 83.56  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNF--AIFRNG-RLLLADDMGLGKTIQAICVAAY---YRK-EWPLLVVTPSSVRFTWAEAFHRWLPSLRpgs 537
Cdd:cd18064    16 LRDYQVRGLNWliSLYENGiNGILADEMGLGKTLQTISLLGYmkhYRNiPGPHMVLVPKSTLHNWMAEFKRWVPTLR--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 tNVIVTGKDNLTGSLIN-----------IISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLLKAARrvI 605
Cdd:cd18064    93 -AVCLIGDKDQRAAFVRdvllpgewdvcVTSYEMLIKEKSVFKKfNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNR--L 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 606 LLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGlRYCDAKqmpwgwDYSGSSNLAELKILLEESIMIRRLKSDVLSQLPA 685
Cdd:cd18064   170 LLTGTPLQNNLHELWALLNFLLPDVFNSAEDFD-SWFDTN------NCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPP 242

                  ..
gi 1944867412 686 KQ 687
Cdd:cd18064   243 KK 244
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
465-634 2.52e-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: 81.22  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGRL---LLADDMGLGKTIQAICVAA--YYRKEW--PLLVVTPSSVRFTWAEAFHRWLPSLR--- 534
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRvggILGDEMGLGKTIQIIAFLAalHHSKLGlgPSLIVCPATVLKQWVKEFHRWWPPFRvvv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 535 ---------PGSTNVIVTGKDNL------TGSLInIISFDLLSKMDKQLKNT-FQVVIIDESHYLKNVKtARCRAAMPLL 598
Cdd:cd18000    81 lhssgsgtgSEEKLGSIERKSQLirkvvgDGGIL-ITTYEGFRKHKDLLLNHnWQYVILDEGHKIRNPD-AEITLACKQL 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1944867412 599 KAARRVIlLSGTPAMSRPMELYTQIaavqpDF-FPQF 634
Cdd:cd18000   159 RTPHRLI-LSGTPIQNNLKELWSLF-----DFvFPPY 189
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
465-634 3.38e-17

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: 81.63  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVN--FAIFR---NGrlLLADDMGLGKTIQAICVAAY---YRKEW-PLLVVTPSSVRFTWAEAFHRWLPSL-- 533
Cdd:cd18003     1 LREYQHIGLDwlATLYEknlNG--ILADEMGLGKTIQTIALLAHlacEKGNWgPHLIVVPTSVMLNWEMEFKRWCPGFki 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 534 ------------------RPGSTNVIVTgkdnltgsliniiSFDLLSKmDKQL--KNTFQVVIIDESHYLKNVKTARCRA 593
Cdd:cd18003    79 ltyygsakerklkrqgwmKPNSFHVCIT-------------SYQLVVQ-DHQVfkRKKWKYLILDEAHNIKNFKSQRWQT 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1944867412 594 AMPLlkAARRVILLSGTPAMSRPMELYT-------QIAAVQPDFFPQF 634
Cdd:cd18003   145 LLNF--NTQRRLLLTGTPLQNSLMELWSlmhflmpHIFQSHQEFKEWF 190
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
465-628 3.59e-17

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: 82.04  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNF--AIFRNGR-LLLADDMGLGKTIQAIC-VAAYYRKEW-----------------------PLLVVTPSS 517
Cdd:cd18005     1 LRDYQREGVEFmyDLYKNGRgGILGDDMGLGKTVQVIAfLAAVLGKTGtrrdrennrprfkkkppassakkPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 518 VRFTWAEAFHRWlpslrpGSTNVIV----TGKDNLTGSL------INIISFDLLSKMDKQLKN-TFQVVIIDESHYLKNV 586
Cdd:cd18005    81 VLYNWKDELDTW------GHFEVGVyhgsRKDDELEGRLkagrleVVVTTYDTLRRCIDSLNSiNWSAVIADEAHRIKNP 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1944867412 587 KTARCRaAMPLLKAARRvILLSGTPAMSRPMELYTQIAAVQP 628
Cdd:cd18005   155 KSKLTQ-AMKELKCKVR-IGLTGTLLQNNMKELWCLLDWAVP 194
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
467-624 3.80e-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: 81.24  E-value: 3.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 467 PFQREGVNFAIFRNGRLLLADdMGLGKTIQAICVAAYYRKEW---PLLVVTPSSV-RFTWAEAFHRWlPSLRPGSTNVIV 542
Cdd:cd18013     3 PYQKVAINFIIEHPYCGLFLD-MGLGKTVTTLTALSDLQLDDftrRVLVIAPLRVaRSTWPDEVEKW-NHLRNLTVSVAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 543 TGKDNLTGSL-----INIISFDLLSKMDKQLKNTFQ--VVIIDESHYLKNVKTARCRAAMPLLKAARRVILLSGTPAMSR 615
Cdd:cd18013    81 GTERQRSKAAntpadLYVINRENLKWLVNKSGDPWPfdMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIGLTGTPSPNG 160

                  ....*....
gi 1944867412 616 PMELYTQIA 624
Cdd:cd18013   161 LMDLWAQIA 169
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
465-620 6.69e-17

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: 80.88  E-value: 6.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNF--AIFRNGR-LLLADDMGLGKTIQAIC-VAAYYRKEW--PLLVVTPSSVRFTWAEAFHRWLPSLrpgst 538
Cdd:cd18001     1 LYPHQREGVAWlwSLHDGGKgGILADDMGLGKTVQICAfLSGMFDSGLikSVLVVMPTSLIPHWVKEFAKWTPGL----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 539 NVIV------TGKDN-----LTGSLINIISFDLLSKMDKQLKNTFQ------VVIIDESHYLKNVKT--ARCRAAMPllk 599
Cdd:cd18001    76 RVKVfhgtskKERERnleriQRGGGVLLTTYGMVLSNTEQLSADDHdefkwdYVILDEGHKIKNSKTksAKSLREIP--- 152
                         170       180
                  ....*....|....*....|.
gi 1944867412 600 aARRVILLSGTPAMSRPMELY 620
Cdd:cd18001   153 -AKNRIILTGTPIQNNLKELW 172
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
468-631 1.64e-16

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: 79.32  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 468 FQREGVNFAIF---RNGRLLLADDMGLGKTIQAICVAAYYRKEW----PLLVVTPSSVRFTWAEAFHRWLPSLrpgstNV 540
Cdd:cd17993     5 YQLTGLNWLAHswcKGNNGILADEMGLGKTVQTISFLSYLFHSQqqygPFLVVVPLSTMPAWQREFAKWAPDM-----NV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 541 IVTGKDNLTGSLI---------------NII--SFDLLSKmDKQLKNTF--QVVIIDESHYLKNvKTARCRAAMPLLKAA 601
Cdd:cd17993    80 IVYLGDIKSRDTIreyefyfsqtkklkfNVLltTYEIILK-DKAFLGSIkwQYLAVDEAHRLKN-DESLLYEALKEFKTN 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 1944867412 602 RRvILLSGTPAMSRPMELYTQIAAVQPDFF 631
Cdd:cd17993   158 NR-LLITGTPLQNSLKELWALLHFLMPGKF 186
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
465-674 1.85e-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: 79.40  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFR----NGrLLLADDMGLGKTIQAICVAAYYRK----EWPLLVVTPSSVRFTWAEAFHRWLPSLRpg 536
Cdd:cd18006     1 LRPYQLEGVNWLLQCraeqHG-CILGDEMGLGKTCQTISLLWYLAGrlklLGPFLVLCPLSVLDNWKEELNRFAPDLS-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 537 stnVIVTGKD-----NLTGSLINIISFD-LLSKMDKQLKNT-------FQVVIIDESHYLKNvKTARCRAAMPLLKAARR 603
Cdd:cd18006    78 ---VITYMGDkekrlDLQQDIKSTNRFHvLLTTYEICLKDAsflksfpWASLVVDEAHRLKN-QNSLLHKTLSEFSVDFR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1944867412 604 vILLSGTPAMSRPMELYTQIAAVQPDFFP--QFHTFGLRYCDAKQmpwgwdysGSSNLAELKILLeESIMIRR 674
Cdd:cd18006   154 -LLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAYSETDD--------ESETVEELHLLL-QPFLLRR 216
HELICc smart00490
helicase superfamily c-terminal domain;
768-851 5.38e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 73.79  E-value: 5.38e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412  768 DAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQlsEKQAVAVLSLTAANMGLTLSAADLVVFAELFWNPGVLIQAEDRA 847
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 1944867412  848 HRIG 851
Cdd:smart00490  79 GRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
464-831 1.03e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 81.61  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 464 SLMPFQREGVN--FAIFRNG--RLLLADDMGLGKTIQAICVAAYYRKEWPLLVVTPS-SVRFTWAEAFHRWLPslrpgst 538
Cdd:COG1061    80 ELRPYQQEALEalLAALERGggRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRrELLEQWAEELRRFLG------- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 539 NVIVTGKDNLTGSLINIISFDLLSKMD--KQLKNTFQVVIIDESHylkNVKTARCRAAMPLLKAARRvILLSGTP----A 612
Cdd:COG1061   153 DPLAGGGKKDSDAPITVATYQSLARRAhlDELGDRFGLVIIDEAH---HAGAPSYRRILEAFPAAYR-LGLTATPfrsdG 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 613 MSRPMELYTQIAavqpdffpqfhtFGLRYCDAKQMpwGWdysgssnLAELKILleesimirrlksDVLSQLPAKQRKMvv 692
Cdd:COG1061   229 REILLFLFDGIV------------YEYSLKEAIED--GY-------LAPPEYY------------GIRVDLTDERAEY-- 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 693 vspEGINAKTKAALAveakkmakgygnkqqekealllfynRTAEAKIHSVVEYILEllESGKDKFLVFAHHKIMLDAIVE 772
Cdd:COG1061   274 ---DALSERLREALA-------------------------ADAERKDKILRELLRE--HPDDRKTLVFCSSVDHAEALAE 323
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1944867412 773 ELEKKRVEYIRIDGSTSSAERQSLCQKFQLSEKQAVAVLSLtaANMGLTLSAADLVVFA 831
Cdd:COG1061   324 LLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDV--LNEGVDVPRLDVAILL 380
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
465-637 2.75e-15

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: 76.58  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNF---AIFRNGRLLLADDMGLGKTIQAICVAAY----YRKEWPLLVVTPSSVRFTWAEAFHRWLPSLrpgs 537
Cdd:cd18054    21 LRDYQLEGLNWlahSWCKNNSVILADEMGLGKTIQTISFLSYlfhqHQLYGPFLLVVPLSTLTSWQREFEIWAPEI---- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 tNVIVTGKDnlTGSLINIISFDLLSKMDKQLK-----NTFQVVI---------------IDESHYLKNVKTARCRAAMPL 597
Cdd:cd18054    97 -NVVVYIGD--LMSRNTIREYEWIHSQTKRLKfnaliTTYEILLkdktvlgsinwaflgVDEAHRLKNDDSLLYKTLIDF 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1944867412 598 LKAARrvILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTF 637
Cdd:cd18054   174 KSNHR--LLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF 211
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
465-643 8.12e-15

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: 74.01  E-value: 8.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGR---LLLADDMGLGKTIQAICVAAYYRKE----WPLLVVTPSSVRFTWAEAFHRWLPSLrpgs 537
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQgtdTILADEMGLGKTIQTIVFLYSLYKEghskGPFLVSAPLSTIINWEREFEMWAPDF---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 tnVIVTgkdnLTGSLINIISFDLLSkMDKQLKNT--FQVVIIDESHYLKNVKTARCRaAMPLLKAARRViLLSGTPAMSR 615
Cdd:cd17994    77 --YVVT----YVGDHVLLTSYELIS-IDQAILGSidWAVLVVDEAHRLKNNQSKFFR-ILNSYKIGYKL-LLTGTPLQNN 147
                         170       180
                  ....*....|....*....|....*...
gi 1944867412 616 PMELYTQIAAVQPDFFPQFHTFGLRYCD 643
Cdd:cd17994   148 LEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
464-631 1.18e-14

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: 74.67  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 464 SLMPFQREGVNFAI--FRNG-RLLLADDMGLGKTIQAICVAAY---YRK-EWPLLVVTPSSVRFTWAEAFHRWLPSLRPg 536
Cdd:cd18065    15 TLRDYQVRGLNWMIslYENGvNGILADEMGLGKTLQTIALLGYlkhYRNiPGPHMVLVPKSTLHNWMNEFKRWVPSLRA- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 537 stnVIVTGKDNLTGSLIN-----------IISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTaRCRAAMPLLKAARRv 604
Cdd:cd18065    94 ---VCLIGDKDARAAFIRdvmmpgewdvcVTSYEMVIKEKSVFKKfNWRYLVIDEAHRIKNEKS-KLSEIVREFKTTNR- 168
                         170       180
                  ....*....|....*....|....*..
gi 1944867412 605 ILLSGTPAMSRPMELYTQIAAVQPDFF 631
Cdd:cd18065   169 LLLTGTPLQNNLHELWALLNFLLPDVF 195
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
480-637 6.42e-14

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: 72.15  E-value: 6.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 480 NGrlLLADDMGLGKTIQAICVAAYYRKE---W-PLLVVTPSSVRFTWAEAFHRWLPSLR-------PGSTNVI------- 541
Cdd:cd18002    21 NG--ILADEMGLGKTVQSIAVLAHLAEEhniWgPFLVIAPASTLHNWQQEISRFVPQFKvlpywgnPKDRKVLrkfwdrk 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 542 -VTGKDnlTGSLINIISFDLLSKMDKQLKNT-FQVVIIDESHYLKNVKTARCRAAMPLlkAARRVILLSGTPAMSRPMEL 619
Cdd:cd18002    99 nLYTRD--APFHVVITSYQLVVQDEKYFQRVkWQYMVLDEAQAIKSSSSSRWKTLLSF--HCRNRLLLTGTPIQNSMAEL 174
                         170
                  ....*....|....*...
gi 1944867412 620 YTQIAAVQPDFFPQFHTF 637
Cdd:cd18002   175 WALLHFIMPTLFDSHDEF 192
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
465-641 7.50e-14

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: 72.50  E-value: 7.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFaIFR--NGRL-------LLADDMGLGKTIQAICVAAYYRKEWP--------LLVVTPSSVRFTWAEAFH 527
Cdd:cd18067     1 LRPHQREGVKF-LYRcvTGRRirgshgcIMADEMGLGKTLQCITLMWTLLRQSPqckpeidkAIVVSPSSLVKNWANELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 528 RWL-PSLRPgstnVIVTG--KDNLTGSLIN--------------IISFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTa 589
Cdd:cd18067    80 KWLgGRLQP----LAIDGgsKKEIDRKLVQwasqqgrrvstpvlIISYETFRLHVEVLQKgEVGLVICDEGHRLKNSDN- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1944867412 590 RCRAAMPLLKAARRVIlLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRY 641
Cdd:cd18067   155 QTYQALDSLNTQRRVL-LSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNF 205
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
465-645 8.64e-14

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: 71.60  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFR--NGR-LLLADDMGLGKTIQAIC-VAAYYRK--EWPLLVVTPSSVRFTWAEAFHRWLpslrpgST 538
Cdd:cd18059     1 LREYQLEGVNWLLFNwyNTRnCILADEMGLGKTIQSITfLYEIYLKgiHGPFLVIAPLSTIPNWEREFRTWT------EL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 539 NVIVTGKDNLTGSLIN-----------------------IISFDLLSKMDKQLKNT-FQVVIIDESHYLKNvKTARCRAA 594
Cdd:cd18059    75 NVVVYHGSQASRRTIQlyemyfkdpqgrvikgsykfhaiITTFEMILTDCPELRNIpWRCVVIDEAHRLKN-RNCKLLEG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1944867412 595 MPLLKAARRViLLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAK 645
Cdd:cd18059   154 LKMMDLEHKV-LLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLK 203
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
465-645 1.78e-13

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: 70.84  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFR---NGRLLLADDMGLGKTIQAICVAA--YYRK-EWPLLVVTPSSVRFTWAEAFHRWLpslrpgST 538
Cdd:cd18058     1 LREYQLEGMNWLLFNwynRKNCILADEMGLGKTIQSITFLSeiFLMGiRGPFLIIAPLSTITNWEREFRTWT------EM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 539 NVIVTGKDNLTGSLIN-----------------------IISFDLLSKMDKQLKNT-FQVVIIDESHYLKNvKTARCRAA 594
Cdd:cd18058    75 NAIVYHGSQISRQMIQqyemyyrdeqgnplsgifkfqvvITTFEMILADCPELKKInWSCVIIDEAHRLKN-RNCKLLEG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1944867412 595 MPLLKAARRViLLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAK 645
Cdd:cd18058   154 LKLMALEHKV-LLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLK 203
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
484-637 2.56e-12

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: 68.15  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 484 LLADDMGLGKTIQAICVAAYY----RKEWPLLVVTPSSVRFTWAEAFHRWLPS-------------------LRPGSTNV 540
Cdd:cd18062    46 ILADEMGLGKTIQTIALITYLmehkRINGPFLIIVPLSTLSNWVYEFDKWAPSvvkvsykgspaarrafvpqLRSGKFNV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 541 IVTgkdnltgsliniiSFDLLSKmDKQL--KNTFQVVIIDESHYLKNVKTARCRAAMPLLKAARRViLLSGTPAMSRPME 618
Cdd:cd18062   126 LLT-------------TYEYIIK-DKQIlaKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRL-LLTGTPLQNKLPE 190
                         170
                  ....*....|....*....
gi 1944867412 619 LYTQIAAVQPDFFPQFHTF 637
Cdd:cd18062   191 LWALLNFLLPTIFKSCSTF 209
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
464-637 4.42e-12

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: 67.40  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 464 SLMPFQREGVNFAI-FRNGRL--LLADDMGLGKTIQAICVAAYY----RKEWPLLVVTPSSVRFTWAEAFHRWLPS---- 532
Cdd:cd18063    23 TLKHYQLQGLEWMVsLYNNNLngILADEMGLGKTIQTIALITYLmehkRLNGPYLIIVPLSTLSNWTYEFDKWAPSvvki 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 533 ---------------LRPGSTNVIVTgkdnltgsliniiSFDLLSKmDKQL--KNTFQVVIIDESHYLKNVKTARCRAAM 595
Cdd:cd18063   103 sykgtpamrrslvpqLRSGKFNVLLT-------------TYEYIIK-DKHIlaKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1944867412 596 PLLKAARRvILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTF 637
Cdd:cd18063   169 THYVAPRR-ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTF 209
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
465-645 9.33e-12

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: 65.80  E-value: 9.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFR--NGR-LLLADDMGLGKTIQAIC-VAAYYRK--EWPLLVVTPSSVRFTWAEAFHRWLpslrpgST 538
Cdd:cd18061     1 LREYQLEGLNWLLFNwyNRRnCILADEMGLGKTIQSITfLYEILLTgiRGPFLIIAPLSTIANWEREFRTWT------DL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 539 NVIVTGKDNLTGSLIN-----------------------IISFDLLSKMDKQLKNT-FQVVIIDESHYLKNvKTARCRAA 594
Cdd:cd18061    75 NVVVYHGSLISRQMIQqyemyfrdsqgriirgayrfqaiITTFEMILGGCPELNAIdWRCVIIDEAHRLKN-KNCKLLEG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1944867412 595 MPLLKAARRViLLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAK 645
Cdd:cd18061   154 LKLMNLEHKV-LLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLK 203
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
465-645 2.69e-11

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: 64.30  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFR---NGRLLLADDMGLGKTIQAICVAAYYRK---EWPLLVVTPSSVRFTWAEAFHRWLpslrpgST 538
Cdd:cd18060     1 LREYQLEGVNWLLFNwynRQNCILADEMGLGKTIQSIAFLQEVYNvgiHGPFLVIAPLSTITNWEREFNTWT------EM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 539 NVIVtgkdnLTGSLIN---IISFDLLSKMDK-----------QLKNTFQV---------------VIIDESHYLKNvKTA 589
Cdd:cd18060    75 NTIV-----YHGSLASrqmIQQYEMYCKDSRgrlipgaykfdALITTFEMilsdcpelreiewrcVIIDEAHRLKN-RNC 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1944867412 590 RCRAAMPLLKAARRViLLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCDAK 645
Cdd:cd18060   149 KLLDSLKHMDLEHKV-LLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLK 203
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
484-621 4.54e-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: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 484 LLADDMGLGKTIQAICVAAYYrkewPLLVVTPSSVRFTWAEAFHRwlpSLRPGSTNVIV--TGKDNLTGSLI-------- 553
Cdd:cd18071    52 ILADDMGLGKTLTTISLILAN----FTLIVCPLSVLSNWETQFEE---HVKPGQLKVYTyhGGERNRDPKLLskydivlt 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1944867412 554 --NIISFDLLSKMDKQLKNT-FQVVIIDESHYLKNVKTARCRAAMPlLKAARRVIlLSGTPAMSRPMELYT 621
Cdd:cd18071   125 tyNTLASDFGAKGDSPLHTInWLRVVLDEGHQIRNPNAQQTKAVLN-LSSERRWV-LTGTPIQNSPKDLGS 193
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
484-641 9.09e-11

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: 63.37  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 484 LLADDMGLGKTIQAIC------VAAYYRKEWPLLVVTPSSVRFTWAEAFHRWLPSLRPGST---NVIVTGKDNLTGSL-- 552
Cdd:cd18068    32 ILAHCMGLGKTLQVVTflhtvlLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLKDEEKievNELATYKRPQERSYkl 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 553 --------INIISFDLLS--------KMDKQLKNTFQ---------VVIIDESHYLKNVKTARCRaAMPLLKAARRVIlL 607
Cdd:cd18068   112 qrwqeeggVMIIGYDMYRilaqernvKSREKLKEIFNkalvdpgpdFVVCDEGHILKNEASAVSK-AMNSIRTKRRIV-L 189
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1944867412 608 SGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRY 641
Cdd:cd18068   190 TGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
484-630 3.90e-10

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: 60.98  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 484 LLADDMGLGKTIQAIC---VAAYYRKEWPLLVVTPSSVRFTWAEAFHRWLPS------LRPGSTNVIVTGKDNLTGSLin 554
Cdd:cd18069    32 ILAHSMGLGKTLQVISfldVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPpealpnVRPRPFKVFILNDEHKTTAA-- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 555 iiSFDLLSKMDK------------QLKNTFQVVIIDESHYLKNVKtARCRAAMPLLKAARRVIlLSGTPAMSRPMELYTQ 622
Cdd:cd18069   110 --RAKVIEDWVKdggvllmgyemfRLRPGPDVVICDEGHRIKNCH-ASTSQALKNIRSRRRIV-LTGYPLQNNLIEYWCM 185

                  ....*...
gi 1944867412 623 IAAVQPDF 630
Cdd:cd18069   186 VDFVRPDF 193
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
465-643 1.58e-09

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: 59.31  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIF---RNGRLLLADDMGLGKTIQ-AICVAAYYRK---EWPLLVVTPSSVRFTWAEAFHRWLPSLrpgS 537
Cdd:cd18056     1 LHPYQLEGLNWLRFswaQGTDTILADEMGLGKTVQtAVFLYSLYKEghsKGPFLVSAPLSTIINWEREFEMWAPDM---Y 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 TNVIVTGKDNLTGSLINIISFD--------LLSKMDKQLKNTFQV----------------------VIIDESHYLKNVK 587
Cdd:cd18056    78 VVTYVGDKDSRAIIRENEFSFEdnairggkKASRMKKEASVKFHVlltsyelitidmailgsidwacLIVDEAHRLKNNQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1944867412 588 TARCRAAMPLlkAARRVILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCD 643
Cdd:cd18056   158 SKFFRVLNGY--SLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD 211
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
465-643 9.20e-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: 57.00  E-value: 9.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIF---RNGRLLLADDMGLGKTIQAICVAAYYRKE----WPLLVVTPSSVRFTWAEAFHRWLPSLRpgs 537
Cdd:cd18057     1 LHPYQLEGLNWLRFswaQGTDTILADEMGLGKTVQTIVFLYSLYKEghskGPYLVSAPLSTIINWEREFEMWAPDFY--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 tnVIVTGKDNLTGSLI--NIISFD--------LLSKMDKQLKNTFQV----------------------VIIDESHYLKN 585
Cdd:cd18057    78 --VVTYTGDKESRSVIreNEFSFEdnairsgkKVFRMKKEAQIKFHVlltsyelitidqailgsiewacLVVDEAHRLKN 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 586 VKTARCRaampLLKAAR--RVILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCD 643
Cdd:cd18057   156 NQSKFFR----VLNSYKidYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
465-637 1.35e-08

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: 56.60  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIF---RNGRLLLADDMGLGKTIQAICVAAYYRKEW----PLLVVTPSSVRFTWAEAFHRWLPSLrpgs 537
Cdd:cd18053    21 LRDYQLNGLNWLAHswcKGNSCILADEMGLGKTIQTISFLNYLFHEHqlygPFLLVVPLSTLTSWQREIQTWAPQM---- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 538 tNVIVTGKDNLTGSLI---------------NII--SFDLLSKMDKQLKN-TFQVVIIDESHYLKNVKTARCRAAMPLLK 599
Cdd:cd18053    97 -NAVVYLGDINSRNMIrthewmhpqtkrlkfNILltTYEILLKDKSFLGGlNWAFIGVDEAHRLKNDDSLLYKTLIDFKS 175
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1944867412 600 AARrvILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTF 637
Cdd:cd18053   176 NHR--LLITGTPLQNSLKELWSLLHFIMPEKFSSWEDF 211
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
465-674 2.12e-08

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 55.95  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGRL----LLADDMGLGKTIQAICVAAYYR-----------KEWPL---------------LVVT 514
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKprggILADDMGLGKTLTMIALILAQKntqnrkeeekeKALTEweskkdstlvpsagtLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 515 PSSVRFTWAEAFHRwlpSLRPGSTNVIV-------TGKDNLTGSLINIISFDLLSKMDKQLKNT------FQV----VII 577
Cdd:cd18072    81 PASLVHQWKNEVES---RVASNKLRVCLyhgpnreRIGEVLRDYDIVITTYSLVAKEIPTYKEEsrssplFRIawarIIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 578 DESHYLKNVKTARCRAAMPLLKAARRVilLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGlRYCDAKQMpwgwdySGSS 657
Cdd:cd18072   158 DEAHNIKNPKVQASIAVCKLRAHARWA--LTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWK-KQVDNKSR------KGGE 228
                         250
                  ....*....|....*..
gi 1944867412 658 NLAelkiLLEESIMIRR 674
Cdd:cd18072   229 RLN----ILTKSLLLRR 241
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
468-643 3.60e-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: 52.32  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 468 FQREGVNFAIF---RNGRLLLADDMGLGKTIQAICVAAYYRKE----WPLLVVTPSSVRFTWAEAFHRWLPSLRpgstnV 540
Cdd:cd18055     4 YQLEGLNWLRFswaQGTDTILADEMGLGKTIQTIVFLYSLYKEghtkGPFLVSAPLSTIINWEREFQMWAPDFY-----V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 541 IVTGKDNLTGSLI--NIISFDLLS--------KMDKQLKNTFQV----------------------VIIDESHYLKNVKT 588
Cdd:cd18055    79 VTYTGDKDSRAIIreNEFSFDDNAvkggkkafKMKREAQVKFHVlltsyelvtidqaalgsirwacLVVDEAHRLKNNQS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1944867412 589 ARCRaampLLKAAR--RVILLSGTPAMSRPMELYTQIAAVQPDFFPQFHTFGLRYCD 643
Cdd:cd18055   159 KFFR----VLNGYKidHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
465-611 8.13e-07

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: 49.61  E-value: 8.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVN--FAIFRNGRLLLADDMGLGKTIQAICVAAYYRKEwPLLVVTPS-SVRFTWAEAFHRWLPSlrpgSTNVI 541
Cdd:cd17926     1 LRPYQEEALEawLAHKNNRRGILVLPTGSGKTLTALALIAYLKEL-RTLIVVPTdALLDQWKERFEDFLGD----SSIGL 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1944867412 542 VTGKDN--LTGSLINIISFDLLSKMDKQLKNTFQ---VVIIDESHYLkNVKTARcraAMPLLKAARRVILLSGTP 611
Cdd:cd17926    76 IGGGKKkdFDDANVVVATYQSLSNLAEEEKDLFDqfgLLIVDEAHHL-PAKTFS---EILKELNAKYRLGLTATP 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
724-868 1.69e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 52.04  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 724 KEALllfyNRTAEAKI-HSVVEYILELLES-----GKDKFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLC 797
Cdd:COG1111   321 RKAM----RLAEEADIeHPKLSKLREILKEqlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEGDKGLT 396
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944867412 798 QKFQLSEKQA-------VAVlSLTAANMGLTLSAADLVVFAELFWNPgvlIQAEDRAHRIGQTSSVNVHYVVAKGTAD 868
Cdd:COG1111   397 QKEQIEILERfragefnVLV-ATSVAEEGLDIPEVDLVIFYEPVPSE---IRSIQRKGRTGRKREGRVVVLIAKGTRD 470
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
465-534 6.88e-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: 48.49  E-value: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 465 LMPFQREGVNFAIFRNGrlLLADDMGLGKTIQAI-CVAAYYRKEWPL----------------------------LVVTP 515
Cdd:cd18070     1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLaLILLHPRPDNDLdaadddsdemvccpdclvaetpvsskatLIVCP 78
                          90       100
                  ....*....|....*....|
gi 1944867412 516 SSVRFTWAEAFHRWLP-SLR 534
Cdd:cd18070    79 SAILAQWLDEINRHVPsSLK 98
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
715-829 1.82e-04

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 43.01  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 715 KGYGNKQQEKEALLLFYNrtAEAKIhSVVEYILELLESGkDKFLVFAHHKIMLDAIVEELEKKRveyirIDGSTSSAERQ 794
Cdd:cd18789    14 REYLGLGAHRKRRLLAAM--NPNKL-RALEELLKRHEQG-DKIIVFTDNVEALYRYAKRLLKPF-----ITGETPQSERE 84
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1944867412 795 SLCQKFQLSEKQAVaVLSlTAANMGLTLSAADLVV 829
Cdd:cd18789    85 EILQNFREGEYNTL-VVS-KVGDEGIDLPEANVAI 117
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
805-862 7.97e-03

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 36.14  E-value: 7.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1944867412 805 KQAVAVLSLTA-ANMGLTLSAADLVVFAELFWNPGVLIQAEDRAHRIGQTSSVnVHYVV 862
Cdd:cd18785    20 ASSLEILVATNvLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE-VILFV 77
ResIII pfam04851
Type III restriction enzyme, res subunit;
464-611 9.03e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 464 SLMPFQREGV----NFAIFRNGRLLLADDMGLGKTIQAICVAAYYRKEWPL---LVVTPS-SVRFTWAEAFHRWLPSlrP 535
Cdd:pfam04851   3 ELRPYQIEAIenllESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIkkvLFLVPRkDLLEQALEEFKKFLPN--Y 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 536 GSTNVIVTGKDNLTGSLINIISF--------DLLSKMDKQLKNTFQVVIIDESHYL-----KNVKTArcraamplLKAAR 602
Cdd:pfam04851  81 VEIGEIISGDKKDESVDDNKIVVttiqslykALELASLELLPDFFDVIIIDEAHRSgassyRNILEY--------FKPAF 152

                  ....*....
gi 1944867412 603 RvILLSGTP 611
Cdd:pfam04851 153 L-LGLTATP 160
PRK13766 PRK13766
Hef nuclease; Provisional
738-872 9.65e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.86  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 738 KIHSVVEYILELLESGKD-KFLVFAHHKIMLDAIVEELEKKRVEYIRIDGSTSSAERQSLCQKFQlseKQAVA------- 809
Cdd:PRK13766  348 KLEKLREIVKEQLGKNPDsRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQASKDGDKGMSQKEQ---IEILDkfragef 424
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944867412 810 -VL-SLTAANMGLTLSAADLVVFAElfwnPgvlIQAEDRA-HRIGQT---SSVNVHYVVAKGTADD-FLW 872
Cdd:PRK13766  425 nVLvSTSVAEEGLDIPSVDLVIFYE----P---VPSEIRSiQRKGRTgrqEEGRVVVLIAKGTRDEaYYW 487
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH