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Conserved domains on  [gi|25148958|ref|NP_498401|]
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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 homolog [Caenorhabditis elegans]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12785020)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
196-408 2.98e-106

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: 321.46  E-value: 2.98e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGRILLADEMGLGKSVQALTIARYYKADWPLLIVCPASVKGAWKKQLNTFFPII--HRIFIVDKS 273
Cdd:cd18010   1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLppDDIQVIVKS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 274 SDPLPdvCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKVALHVILLSGTPALSRPSEL 353
Cdd:cd18010  81 KDGLR--DGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIEL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25148958 354 FTQIRLIDHKLFTNFHEFAIRYCDGKQGRFCFEAKGCTNSEELAAIMFKRLMIRR 408
Cdd:cd18010 159 FTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
470-597 3.94e-41

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


:

Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 146.47  E-value: 3.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 470 KAAAVCEHILENYfypdAPPRKVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIRVAVLSIT 549
Cdd:cd18793  12 KLEALLELLEELR----EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 25148958 550 AAGVGITLTAASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFVQYLI 597
Cdd:cd18793  88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
114-165 6.70e-14

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: 66.42  E-value: 6.70e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25148958   114 PFHSAVIDLIKQVPSRNYDPAKRSWTVASSDHitiSNILKNATAV-KVELEPL 165
Cdd:pfam07443   6 GYHAELIAVFKQMPSRNYDPKTKKWNFSLEDY---SKLMEAARALpQVELEPL 55
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
196-408 2.98e-106

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: 321.46  E-value: 2.98e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGRILLADEMGLGKSVQALTIARYYKADWPLLIVCPASVKGAWKKQLNTFFPII--HRIFIVDKS 273
Cdd:cd18010   1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLppDDIQVIVKS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 274 SDPLPdvCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKVALHVILLSGTPALSRPSEL 353
Cdd:cd18010  81 KDGLR--DGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIEL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25148958 354 FTQIRLIDHKLFTNFHEFAIRYCDGKQGRFCFEAKGCTNSEELAAIMFKRLMIRR 408
Cdd:cd18010 159 FTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
196-620 2.92e-90

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.60  E-value: 2.92e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFAL---ERDGRILLADEMGLGKSVQALTIARYYKA---DWPLLIVCPASVKGAWKKQLNTFFPIIhRIFI 269
Cdd:COG0553 242 LRPYQLEGAAWLLflrRLGLGGLLADDMGLGKTIQALALLLELKErglARPVLIVAPTSLVGNWQRELAKFAPGL-RVLV 320
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 270 VDKSSD--PLPDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVILLSGTPAL 347
Cdd:COG0553 321 LDGTREraKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK--ARHRLALTGTPVE 398
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 348 SRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKqgrfcfEAKGCTNSEELAAIMfKRLMIRRLKADVLKDLPEKRREVVYV 427
Cdd:COG0553 399 NRLEELWSLLDFLNPGLLGSLKAFRERFARPI------EKGDEEALERLRRLL-RPFLLRRTKEDVLKDLPEKTEETLYV 471
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 428 SgptidarMDDLQKARadYEKVNSMERKH-ESLLEFYS----LTGIVKAAAVCEH-----------------------IL 479
Cdd:COG0553 472 E-------LTPEQRAL--YEAVLEYLRRElEGAEGIRRrgliLAALTRLRQICSHpallleegaelsgrsaklealleLL 542
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 480 ENYFypdAPPRKVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIRVAVLSITAAGVGITLTA 559
Cdd:COG0553 543 EELL---AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTA 619
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25148958 560 ASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFVQYLIAKKTADDVMWNMVQQKLDVLGQV 620
Cdd:COG0553 620 ADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESV 680
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
470-597 3.94e-41

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 146.47  E-value: 3.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 470 KAAAVCEHILENYfypdAPPRKVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIRVAVLSIT 549
Cdd:cd18793  12 KLEALLELLEELR----EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 25148958 550 AAGVGITLTAASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFVQYLI 597
Cdd:cd18793  88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
199-441 1.81e-31

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: 124.33  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   199 YQKEGVIFALERD-GRI---LLADEMGLGKSVQALTIARY---YKADW--PLLIVCPASVKGAWKKQLNTF--FPIIhRI 267
Cdd:pfam00176   1 YQIEGVNWMLSLEnNLGrggILADEMGLGKTLQTISLLLYlkhVDKNWggPTLIVVPLSLLHNWMNEFERWvsPPAL-RV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   268 FIVDKSSDPLPDVCTSNTVA------IMSYEqMVLKH-DILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVIL 340
Cdd:pfam00176  80 VVLHGNKRPQERWKNDPNFLadfdvvITTYE-TLRKHkELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK--TRNRWI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   341 LSGTPALSRPSELFTQIRLIDHKLFTNFHEFairycdgKQGR-FCFEAKGCT-NSEELAAIMfKRLMIRRLKADVLKDLP 418
Cdd:pfam00176 157 LTGTPLQNNLEELWALLNFLRPGPFGSLSTF-------RNWFdRPIERGGGKkGVSRLHKLL-KPFLLRRTKKDVEKSLP 228
                         250       260
                  ....*....|....*....|...
gi 25148958   419 EKRREVVYVsgptidaRMDDLQK 441
Cdd:pfam00176 229 PKVEYILFC-------RLSKLQR 244
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
215-593 2.33e-31

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 131.08  E-value: 2.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   215 LLADEMGLGKSVQALTI----ARYYKADWPLLIVCPASVKGAWKKQLNTFFPII----------HRIFIVDKSSDPLP-D 279
Cdd:PLN03142  192 ILADEMGLGKTLQTISLlgylHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLravkfhgnpeERAHQREELLVAGKfD 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   280 VCtsntvaIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVILLSGTPALSRPSELFTQIRL 359
Cdd:PLN03142  272 VC------VTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFS--TNYRLLITGTPLQNNLHELWALLNF 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   360 IDHKLFTN---FHEFairycdgkqgrfcFEAKGCTNSEELAAIMFKRL---MIRRLKADVLKDLPEKRREVVYVSgptid 433
Cdd:PLN03142  344 LLPEIFSSaetFDEW-------------FQISGENDQQEVVQQLHKVLrpfLLRRLKSDVEKGLPPKKETILKVG----- 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   434 arMDDLQKA------RADYEKVNS-MERKHesllefysLTGIVKAAAVC-------------------EHILENY----- 482
Cdd:PLN03142  406 --MSQMQKQyykallQKDLDVVNAgGERKR--------LLNIAMQLRKCcnhpylfqgaepgppyttgEHLVENSgkmvl 475
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   483 ---FYPDAPPR--KVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIR-VAVLSITAAGVGIT 556
Cdd:PLN03142  476 ldkLLPKLKERdsRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGIN 555
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 25148958   557 LTAASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFV 593
Cdd:PLN03142  556 LATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQV 592
DEXDc smart00487
DEAD-like helicases superfamily;
190-345 1.30e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.47  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958    190 PSLIERLFPYQKEGVIFALERDGRILLADEMGLGKSVQALTIARYY---KADWPLLIVCP-ASVKGAWKKQLNTFFPIIH 265
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrGKGGRVLVLVPtRELAEQWAEELKKLGPSLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958    266 RI---FIVDKSSDPLPDVCTSNT--VAIMSYEQMV--LKHDILKKEKYRTIIFDESHMLKDGKARR--TKVATDLSKvAL 336
Cdd:smart00487  83 LKvvgLYGGDSKREQLRKLESGKtdILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGGFGDqlEKLLKLLPK-NV 161

                   ....*....
gi 25148958    337 HVILLSGTP 345
Cdd:smart00487 162 QLLLLSATP 170
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
114-165 6.70e-14

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: 66.42  E-value: 6.70e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25148958   114 PFHSAVIDLIKQVPSRNYDPAKRSWTVASSDHitiSNILKNATAV-KVELEPL 165
Cdd:pfam07443   6 GYHAELIAVFKQMPSRNYDPKTKKWNFSLEDY---SKLMEAARALpQVELEPL 55
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
470-586 6.97e-14

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: 68.01  E-value: 6.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   470 KAAAVCEHILENyfypdaPPRKVLIFAHHQIVLDTIQVEvNKRKLGSIRIDGKTPSHRRTALCDSFQtDDNIRVaVLSIT 549
Cdd:pfam00271   2 KLEALLELLKKE------RGGKVLIFSQTKKTLEAELLL-EKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATD 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 25148958   550 AAGVGITLTAASVVVFAEIHFNPGYLVQAEDRAHRVG 586
Cdd:pfam00271  73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
503-586 1.10e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 61.07  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958    503 DTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNirVAVLSITAAGVGITLTAASVVVFAEIHFNPGYLVQAEDRA 582
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 25148958    583 HRVG 586
Cdd:smart00490  79 GRAG 82
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
196-408 2.98e-106

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: 321.46  E-value: 2.98e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGRILLADEMGLGKSVQALTIARYYKADWPLLIVCPASVKGAWKKQLNTFFPII--HRIFIVDKS 273
Cdd:cd18010   1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLppDDIQVIVKS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 274 SDPLPdvCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKVALHVILLSGTPALSRPSEL 353
Cdd:cd18010  81 KDGLR--DGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIEL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25148958 354 FTQIRLIDHKLFTNFHEFAIRYCDGKQGRFCFEAKGCTNSEELAAIMFKRLMIRR 408
Cdd:cd18010 159 FTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
196-620 2.92e-90

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.60  E-value: 2.92e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFAL---ERDGRILLADEMGLGKSVQALTIARYYKA---DWPLLIVCPASVKGAWKKQLNTFFPIIhRIFI 269
Cdd:COG0553 242 LRPYQLEGAAWLLflrRLGLGGLLADDMGLGKTIQALALLLELKErglARPVLIVAPTSLVGNWQRELAKFAPGL-RVLV 320
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 270 VDKSSD--PLPDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVILLSGTPAL 347
Cdd:COG0553 321 LDGTREraKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK--ARHRLALTGTPVE 398
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 348 SRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKqgrfcfEAKGCTNSEELAAIMfKRLMIRRLKADVLKDLPEKRREVVYV 427
Cdd:COG0553 399 NRLEELWSLLDFLNPGLLGSLKAFRERFARPI------EKGDEEALERLRRLL-RPFLLRRTKEDVLKDLPEKTEETLYV 471
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 428 SgptidarMDDLQKARadYEKVNSMERKH-ESLLEFYS----LTGIVKAAAVCEH-----------------------IL 479
Cdd:COG0553 472 E-------LTPEQRAL--YEAVLEYLRRElEGAEGIRRrgliLAALTRLRQICSHpallleegaelsgrsaklealleLL 542
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 480 ENYFypdAPPRKVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIRVAVLSITAAGVGITLTA 559
Cdd:COG0553 543 EELL---AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTA 619
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25148958 560 ASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFVQYLIAKKTADDVMWNMVQQKLDVLGQV 620
Cdd:COG0553 620 ADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESV 680
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
470-597 3.94e-41

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 146.47  E-value: 3.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 470 KAAAVCEHILENYfypdAPPRKVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIRVAVLSIT 549
Cdd:cd18793  12 KLEALLELLEELR----EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 25148958 550 AAGVGITLTAASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFVQYLI 597
Cdd:cd18793  88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
196-361 1.44e-37

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: 138.08  E-value: 1.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERD---GRILLADEMGLGKSVQALTIARY----YKADWPLLIVCPASVKGAWKKQLNTFFPIIhRIF 268
Cdd:cd17919   1 LRPYQLEGLNFLLELYengPGGILADEMGLGKTLQAIAFLAYllkeGKERGPVLVVCPLSVLENWEREFEKWTPDL-RVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 269 IVDKSSDP------LPDVCTSNtVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVILLS 342
Cdd:cd17919  80 VYHGSQREraqiraKEKLDKFD-VVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR--AKRRLLLT 156
                       170
                ....*....|....*....
gi 25148958 343 GTPALSRPSELFTQIRLID 361
Cdd:cd17919 157 GTPLQNNLEELWALLDFLD 175
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
199-441 1.81e-31

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: 124.33  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   199 YQKEGVIFALERD-GRI---LLADEMGLGKSVQALTIARY---YKADW--PLLIVCPASVKGAWKKQLNTF--FPIIhRI 267
Cdd:pfam00176   1 YQIEGVNWMLSLEnNLGrggILADEMGLGKTLQTISLLLYlkhVDKNWggPTLIVVPLSLLHNWMNEFERWvsPPAL-RV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   268 FIVDKSSDPLPDVCTSNTVA------IMSYEqMVLKH-DILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVIL 340
Cdd:pfam00176  80 VVLHGNKRPQERWKNDPNFLadfdvvITTYE-TLRKHkELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK--TRNRWI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   341 LSGTPALSRPSELFTQIRLIDHKLFTNFHEFairycdgKQGR-FCFEAKGCT-NSEELAAIMfKRLMIRRLKADVLKDLP 418
Cdd:pfam00176 157 LTGTPLQNNLEELWALLNFLRPGPFGSLSTF-------RNWFdRPIERGGGKkGVSRLHKLL-KPFLLRRTKKDVEKSLP 228
                         250       260
                  ....*....|....*....|...
gi 25148958   419 EKRREVVYVsgptidaRMDDLQK 441
Cdd:pfam00176 229 PKVEYILFC-------RLSKLQR 244
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
215-593 2.33e-31

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 131.08  E-value: 2.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   215 LLADEMGLGKSVQALTI----ARYYKADWPLLIVCPASVKGAWKKQLNTFFPII----------HRIFIVDKSSDPLP-D 279
Cdd:PLN03142  192 ILADEMGLGKTLQTISLlgylHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLravkfhgnpeERAHQREELLVAGKfD 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   280 VCtsntvaIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVILLSGTPALSRPSELFTQIRL 359
Cdd:PLN03142  272 VC------VTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFS--TNYRLLITGTPLQNNLHELWALLNF 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   360 IDHKLFTN---FHEFairycdgkqgrfcFEAKGCTNSEELAAIMFKRL---MIRRLKADVLKDLPEKRREVVYVSgptid 433
Cdd:PLN03142  344 LLPEIFSSaetFDEW-------------FQISGENDQQEVVQQLHKVLrpfLLRRLKSDVEKGLPPKKETILKVG----- 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   434 arMDDLQKA------RADYEKVNS-MERKHesllefysLTGIVKAAAVC-------------------EHILENY----- 482
Cdd:PLN03142  406 --MSQMQKQyykallQKDLDVVNAgGERKR--------LLNIAMQLRKCcnhpylfqgaepgppyttgEHLVENSgkmvl 475
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   483 ---FYPDAPPR--KVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIR-VAVLSITAAGVGIT 556
Cdd:PLN03142  476 ldkLLPKLKERdsRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGIN 555
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 25148958   557 LTAASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFV 593
Cdd:PLN03142  556 LATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQV 592
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
196-371 8.58e-27

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: 108.53  E-value: 8.58e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERD-GRILLADEMGLGKSVQALTIARYYKADW---PLLIVCPASVKGAWKKQLNTFFPIihRIFIVD 271
Cdd:cd18011   1 PLPHQIDAVLRALRKPpVRLLLADEVGLGKTIEAGLIIKELLLRGdakRVLILCPASLVEQWQDELQDKFGL--PFLILD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 272 KSS-----DPLPDVCTSNTVAIMSYEQmvLKHDI-----LKKEKYRTIIFDESHMLK----DGKARRTKVATDLSKVALH 337
Cdd:cd18011  79 RETaaqlrRLIGNPFEEFPIVIVSLDL--LKRSEerrglLLSEEWDLVVVDEAHKLRnsggGKETKRYKLGRLLAKRARH 156
                       170       180       190
                ....*....|....*....|....*....|....
gi 25148958 338 VILLSGTPALSRPSELFTQIRLIDHKLFTNFHEF 371
Cdd:cd18011 157 VLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRF 190
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
196-410 3.61e-25

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 104.18  E-value: 3.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV--IFALERDG-RILLADEMGLGKSVQALTIARYYKADW---PLLIVCPASVKGAWKKQLNTFFP-----II 264
Cdd:cd18012   5 LRPYQKEGFnwLSFLRHYGlGGILADDMGLGKTLQTLALLLSRKEEGrkgPSLVVAPTSLIYNWEEEAAKFAPelkvlVI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 265 HRifivDKSSDPLPDVCTSNTVAIMSYEqmVLKHDI--LKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVILLS 342
Cdd:cd18012  85 HG----TKRKREKLRALEDYDLVITSYG--LLRRDIelLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALK--ADHRLALT 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25148958 343 GTPALSRPSELFTQIRLI------DHKLFTNFHEFAI-RYCDGKqgrfcfeakgctNSEELAAiMFKRLMIRRLK 410
Cdd:cd18012 157 GTPIENHLGELWSIFDFLnpgllgSYKRFKKRFAKPIeKDGDEE------------ALEELKK-LISPFILRRLK 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
196-408 5.15e-21

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: 92.31  E-value: 5.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALE--RDGR-ILLADEMGLGKSVQALT----IARYYKADWPLLIVCPASVKGAWKKQLNTFFPI----- 263
Cdd:cd17995   1 LRDYQLEGVNWLLFnwYNRRnCILADEMGLGKTIQSIAflehLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMnvvvy 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 264 -----------IHRIFIVDKSSDPLPDVCTSNTVaIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDgkaRRTKVATDLS 332
Cdd:cd17995  81 hgsgesrqiiqQYEMYFKDAQGRKKKGVYKFDVL-ITTYEMVIADAEELRKIPWRVVVVDEAHRLKN---RNSKLLQGLK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25148958 333 KVAL-HVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQGRfcfeakgctNSEELAAIMfKRLMIRR 408
Cdd:cd17995 157 KLTLeHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAE---------QVEKLQALL-KPYMLRR 223
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
196-353 9.81e-20

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: 88.56  E-value: 9.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV--IFALERDG-RILLADEMGLGKSVQALTI---------ARYYKADWPLLIVCPASVKGAWKKQLNTFFPI 263
Cdd:cd17999   1 LRPYQQEGInwLAFLNKYNlHGILCDDMGLGKTLQTLCIlasdhhkraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 264 ----IHRIFIVDKSSDPLPDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLskVALHVI 339
Cdd:cd17999  81 aflkPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQL--KANHRL 158
                       170
                ....*....|....
gi 25148958 340 LLSGTPALSRPSEL 353
Cdd:cd17999 159 ILSGTPIQNNVLEL 172
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
196-361 2.54e-19

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: 86.22  E-value: 2.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALE----RDGRILlADEMGLGKSVQ--ALTIARYY--KADWPLLIVCPASVKGAWKKQLNTFFPIIhRI 267
Cdd:cd18000   1 LFKYQQTGVQWLWElhcqRVGGIL-GDEMGLGKTIQiiAFLAALHHskLGLGPSLIVCPATVLKQWVKEFHRWWPPF-RV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 268 FIVDKS----------------SDPLPDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDL 331
Cdd:cd18000  79 VVLHSSgsgtgseeklgsierkSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
                       170       180       190
                ....*....|....*....|....*....|
gi 25148958 332 SKValHVILLSGTPALSRPSELFTqirLID 361
Cdd:cd18000 159 RTP--HRLILSGTPIQNNLKELWS---LFD 183
DEXDc smart00487
DEAD-like helicases superfamily;
190-345 1.30e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.47  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958    190 PSLIERLFPYQKEGVIFALERDGRILLADEMGLGKSVQALTIARYY---KADWPLLIVCP-ASVKGAWKKQLNTFFPIIH 265
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrGKGGRVLVLVPtRELAEQWAEELKKLGPSLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958    266 RI---FIVDKSSDPLPDVCTSNT--VAIMSYEQMV--LKHDILKKEKYRTIIFDESHMLKDGKARR--TKVATDLSKvAL 336
Cdd:smart00487  83 LKvvgLYGGDSKREQLRKLESGKtdILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGGFGDqlEKLLKLLPK-NV 161

                   ....*....
gi 25148958    337 HVILLSGTP 345
Cdd:smart00487 162 QLLLLSATP 170
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
196-375 4.26e-18

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: 84.26  E-value: 4.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALER-------DGR-ILLADEMGLGKSVQALTIA----RYYKADWPL----LIVCPASVKGAWKKQLNT 259
Cdd:cd18004   1 LRPHQREGVQFLYDCltgrrgyGGGgAILADEMGLGKTLQAIALVwtllKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 260 FFPiIHRIFIVDKSSDPLPDVCTSNT--------VAIMSYEQmVLKH--DILKKEKYRTIIFDESHMLKDGKarrTKVAT 329
Cdd:cd18004  81 WLG-LRRIKVVTADGNAKDVKASLDFfssastypVLIISYET-LRRHaeKLSKKISIDLLICDEGHRLKNSE---SKTTK 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 25148958 330 DLSKV-ALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRY 375
Cdd:cd18004 156 ALNSLpCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVF 202
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
196-408 1.16e-17

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: 82.10  E-value: 1.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGR---ILLADEMGLGKSVQALTIARYY----KADWPLLIVCPASVKGAWKKQLNTFFPIIHRI- 267
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEqhgCILGDEMGLGKTCQTISLLWYLagrlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 268 FIVDKS--SDPLPDVCTSNT--VAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKValHVILLSG 343
Cdd:cd18006  81 YMGDKEkrLDLQQDIKSTNRfhVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVD--FRLLLTG 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25148958 344 TPALSRPSELFTQIRLIDHKLF--TNFHEFAIRYCDGKqgrfcfeaKGCTNSEELAAIMfKRLMIRR 408
Cdd:cd18006 159 TPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSETD--------DESETVEELHLLL-QPFLLRR 216
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
190-421 2.64e-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: 82.02  E-value: 2.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 190 PSLIE--RLFPYQKEGV--IFALERDG-RILLADEMGLGKSVQALTIARYYK----ADWPLLIVCPASVKGAWKKQLNTF 260
Cdd:cd18064   8 PSYVKwgKLRDYQVRGLnwLISLYENGiNGILADEMGLGKTLQTISLLGYMKhyrnIPGPHMVLVPKSTLHNWMAEFKRW 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 261 FPIIHRIFIV-DKSSDP-------LP---DVCtsntvaIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVAT 329
Cdd:cd18064  88 VPTLRAVCLIgDKDQRAafvrdvlLPgewDVC------VTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 330 DLSKValHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFairycdgkqgRFCFEAKGCTNSEELAA---IMFKRLMI 406
Cdd:cd18064 162 EFKTT--NRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDF----------DSWFDTNNCLGDQKLVErlhMVLRPFLL 229
                       250
                ....*....|....*
gi 25148958 407 RRLKADVLKDLPEKR 421
Cdd:cd18064 230 RRIKADVEKSLPPKK 244
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
196-408 4.60e-17

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: 81.18  E-value: 4.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGriLLADEMGLGKSVQAL-TIA--RYYKADWPL------------------LIVCPASVKGAWK 254
Cdd:cd18008   1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALaLILatRPQDPKIPEeleenssdpkklylskttLIVVPLSLLSQWK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 255 KQLNTFF-PIIHRIFIVDKSS-DPLPDVCTSNTVAIMSYEqmVLKHDILKKEK-------------------YRtIIFDE 313
Cdd:cd18008  79 DEIEKHTkPGSLKVYVYHGSKrIKSIEELSDYDIVITTYG--TLASEFPKNKKgggrdskekeasplhrirwYR-VILDE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 314 SHMLKDGKARRTKVATDLSkvALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAirycdgKQGRFCFEAKGCTNS 393
Cdd:cd18008 156 AHNIKNRSTKTSRAVCALK--AERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFN------SDISKPFSKNDRKAL 227
                       250
                ....*....|....*
gi 25148958 394 EELAAIMfKRLMIRR 408
Cdd:cd18008 228 ERLQALL-KPILLRR 241
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
196-355 1.52e-15

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 76.65  E-value: 1.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALER--DGR-ILLADEMGLGKSVQ--ALTIARYYK---------------------ADW-PLLIVCPAS 248
Cdd:cd18005   1 LRDYQREGVEFMYDLykNGRgGILGDDMGLGKTVQviAFLAAVLGKtgtrrdrennrprfkkkppasSAKkPVLIVAPLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 249 VKGAWKKQLNTF--FPI--IHRifiVDKSSDPLPDVCTSNT-VAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKAR 323
Cdd:cd18005  81 VLYNWKDELDTWghFEVgvYHG---SRKDDELEGRLKAGRLeVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                       170       180       190
                ....*....|....*....|....*....|..
gi 25148958 324 RTKVATDLskVALHVILLSGTPALSRPSELFT 355
Cdd:cd18005 158 LTQAMKEL--KCKVRIGLTGTLLQNNMKELWC 187
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
196-361 2.47e-15

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: 76.04  E-value: 2.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIF---------ALERDGRILlADEMGLGKSVQALTIAryykadWPL---------------LIVCPASVKG 251
Cdd:cd18066   1 LRPHQREGIEFlyecvmgmrVNERFGAIL-ADEMGLGKTLQCISLI------WTLlrqgpyggkpvikraLIVTPGSLVK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 252 AWKKQLNTFFPIIH-RIFIVDKSSdPLPDVCTSN--TVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVA 328
Cdd:cd18066  74 NWKKEFQKWLGSERiKVFTVDQDH-KVEEFIASPlySVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL 152
                       170       180       190
                ....*....|....*....|....*....|...
gi 25148958 329 TDLSkvALHVILLSGTPALSRPSELFTQIRLID 361
Cdd:cd18066 153 TSLS--CERRIILTGTPIQNDLQEFFALIDFVN 183
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
215-408 9.92e-15

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: 74.08  E-value: 9.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARY---YKADW-PLLIVCPASVKGAWKKQLNTFFPII---------HRIFIVDKSSDPlPDVC 281
Cdd:cd18002  23 ILADEMGLGKTVQSIAVLAHlaeEHNIWgPFLVIAPASTLHNWQQEISRFVPQFkvlpywgnpKDRKVLRKFWDR-KNLY 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 282 TSNT---VAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKvaTDLSKVALHVILLSGTPALSRPSELFTQIR 358
Cdd:cd18002 102 TRDApfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWK--TLLSFHCRNRLLLTGTPIQNSMAELWALLH 179
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25148958 359 LIDHKLFTNFHEFAIRYCDGKQGRfcFEAKGCTNSEELAAI--MFKRLMIRR 408
Cdd:cd18002 180 FIMPTLFDSHDEFNEWFSKDIESH--AENKTGLNEHQLKRLhmILKPFMLRR 229
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
196-377 1.22e-14

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 73.54  E-value: 1.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGRILLADeMGLGKSVQALTIARYYKADW---PLLIVCPASV-KGAWKKQL---NTFFPIIHRIf 268
Cdd:cd18013   1 PHPYQKVAINFIIEHPYCGLFLD-MGLGKTVTTLTALSDLQLDDftrRVLVIAPLRVaRSTWPDEVekwNHLRNLTVSV- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 269 IVDKSSDPLPDVCTSNTVAIMSYEQMVLKHDILKKE-KYRTIIFDESHMLKDGKARRTKVATDLSKVALHVILLSGTPAL 347
Cdd:cd18013  79 AVGTERQRSKAANTPADLYVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIGLTGTPSP 158
                       170       180       190
                ....*....|....*....|....*....|..
gi 25148958 348 SRPSELFTQIRLIDH--KLFTNFHEFAIRYCD 377
Cdd:cd18013 159 NGLMDLWAQIALLDQgeRLGRSITAYRERWFD 190
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
196-345 1.88e-14

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: 72.03  E-value: 1.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV---IFALERDGRILLADEMGLGKSVQALTIARYYKAD---WPLLIVCPASVKGAWKKQLNTFFPIIH---- 265
Cdd:cd17998   1 LKDYQLIGLnwlNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIgipGPHLVVVPSSTLDNWLREFKRWCPSLKvepy 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 266 ----------RIFIVDKSSDPLPDVCTSNTVAIMSYEQMVLKHdilkkEKYRTIIFDESHMLKDGKARRTKvatDLSKV- 334
Cdd:cd17998  81 ygsqeerkhlRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKR-----LKLNYVVYDEGHMLKNMTSERYR---HLMTIn 152
                       170
                ....*....|.
gi 25148958 335 ALHVILLSGTP 345
Cdd:cd17998 153 ANFRLLLTGTP 163
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
215-371 2.04e-14

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: 73.12  E-value: 2.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARYYK----ADWPLLIVCPASVKGAWKKQLNTFFPIIHRI-----------FIVDKSSDPLPD 279
Cdd:cd17997  26 ILADEMGLGKTLQTISLLGYLKhyknINGPHLIIVPKSTLDNWMREFKRWCPSLRVVvligdkeeradIIRDVLLPGKFD 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 280 VCtsntvaIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKVALhvILLSGTPALSRPSELFTQIRL 359
Cdd:cd17997 106 VC------ITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR--LLLTGTPLQNNLHELWALLNF 177
                       170
                ....*....|..
gi 25148958 360 IDHKLFTNFHEF 371
Cdd:cd17997 178 LLPDVFTSSEDF 189
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
199-408 2.60e-14

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: 72.77  E-value: 2.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEG---VIFALERDGRILLADEMGLGKSVQALTIAR---YYKADWPLLIVCPASVKGAWKKQLNTFFPI--------- 263
Cdd:cd18058   4 YQLEGmnwLLFNWYNRKNCILADEMGLGKTIQSITFLSeifLMGIRGPFLIIAPLSTITNWEREFRTWTEMnaivyhgsq 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 264 IHRIFIV-------DKSSDPLPDVCTSNTVaIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDgkaRRTKVATDLSKVAL 336
Cdd:cd18058  84 ISRQMIQqyemyyrDEQGNPLSGIFKFQVV-ITTFEMILADCPELKKINWSCVIIDEAHRLKN---RNCKLLEGLKLMAL 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25148958 337 -HVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQGRfcfeakgctNSEELAAIMfKRLMIRR 408
Cdd:cd18058 160 eHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEE---------QVKKLQSIL-KPMMLRR 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
199-371 2.80e-14

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: 72.38  E-value: 2.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEGV--IFAL-ERDGRILLADEMGLGKSVQalTIA-----RYYKADW-PLLIVCPASVKGAWKKQLNTFFPIIhRIFI 269
Cdd:cd18003   4 YQHIGLdwLATLyEKNLNGILADEMGLGKTIQ--TIAllahlACEKGNWgPHLIVVPTSVMLNWEMEFKRWCPGF-KILT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 270 VDKSSDPL---------PDvctSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALHVIL 340
Cdd:cd18003  81 YYGSAKERklkrqgwmkPN---SFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN--TQRRLL 155
                       170       180       190
                ....*....|....*....|....*....|.
gi 25148958 341 LSGTPALSRPSELFTQIRLIDHKLFTNFHEF 371
Cdd:cd18003 156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEF 186
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
215-410 3.81e-14

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: 72.40  E-value: 3.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARY---YKADW-PLLIVCPASVKGAWKKQLNTFFPIIHRIFIVDKssdplPDV---------C 281
Cdd:cd17996  26 ILADEMGLGKTIQTISLITYlmeKKKNNgPYLVIVPLSTLSNWVSEFEKWAPSVSKIVYKGT-----PDVrkklqsqirA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 282 TSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDgkaRRTKVATDLSK--VALHVILLSGTPALSRPSELFTQIRL 359
Cdd:cd17996 101 GKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKN---AQSKLTQTLNTyyHARYRLLLTGTPLQNNLPELWALLNF 177
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25148958 360 IDHKLFTN---FHE-----FAIrycDGKQGRFCFeakgctnSEELAAIMFKRL-------MIRRLK 410
Cdd:cd17996 178 LLPKIFKScktFEQwfntpFAN---TGEQVKIEL-------NEEETLLIIRRLhkvlrpfLLRRLK 233
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
196-371 4.49e-14

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: 72.32  E-value: 4.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIF---------ALERDGR-ILLADEMGLGKSVQALTI----ARYYKADWPLLIVCPASVKGAWKKQLNTFF 261
Cdd:cd18007   1 LKPHQVEGVRFlwsnlvgtdVGSDEGGgCILAHTMGLGKTLQVITFlhtyLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 262 PIIHRIFIVDKSSDPLPDVcTSNTVAI-----------MSYE--QMVLKHDILKKEKYRT------------IIFDESHM 316
Cdd:cd18007  81 PPDLRPLLVLVSLSASKRA-DARLRKInkwhkeggvllIGYElfRNLASNATTDPRLKQEfiaalldpgpdlLVLDEGHR 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25148958 317 LKDGKARRTKVatdLSKVALHV-ILLSGTPALSRPSELFTQIRLIDHKLFTNFHEF 371
Cdd:cd18007 160 LKNEKSQLSKA---LSKVKTKRrILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEF 212
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
114-165 6.70e-14

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: 66.42  E-value: 6.70e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25148958   114 PFHSAVIDLIKQVPSRNYDPAKRSWTVASSDHitiSNILKNATAV-KVELEPL 165
Cdd:pfam07443   6 GYHAELIAVFKQMPSRNYDPKTKKWNFSLEDY---SKLMEAARALpQVELEPL 55
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
470-586 6.97e-14

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: 68.01  E-value: 6.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958   470 KAAAVCEHILENyfypdaPPRKVLIFAHHQIVLDTIQVEvNKRKLGSIRIDGKTPSHRRTALCDSFQtDDNIRVaVLSIT 549
Cdd:pfam00271   2 KLEALLELLKKE------RGGKVLIFSQTKKTLEAELLL-EKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATD 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 25148958   550 AAGVGITLTAASVVVFAEIHFNPGYLVQAEDRAHRVG 586
Cdd:pfam00271  73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
196-345 1.20e-13

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: 70.86  E-value: 1.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFA----LERDGRILlADEMGLGKSVQALT----IARYYKADWPLLIVcPASVKGAWKKQLNTFFPIIhRI 267
Cdd:cd18001   1 LYPHQREGVAWLwslhDGGKGGIL-ADDMGLGKTVQICAflsgMFDSGLIKSVLVVM-PTSLIPHWVKEFAKWTPGL-RV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 268 FIVDKSS-----DPLPDVCTSNTVAIMSYeQMV------LKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvAL 336
Cdd:cd18001  78 KVFHGTSkkereRNLERIQRGGGVLLTTY-GMVlsnteqLSADDHDEFKWDYVILDEGHKIKNSKTKSAKSLREIP--AK 154

                ....*....
gi 25148958 337 HVILLSGTP 345
Cdd:cd18001 155 NRIILTGTP 163
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
195-584 4.65e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 72.36  E-value: 4.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 195 RLFPYQKEgvifALER--------DGRILLADEMGLGKSVQALTIARYYKADWPLLIVCP-ASVKGAWKKQLNTFFPIIH 265
Cdd:COG1061  80 ELRPYQQE----ALEAllaalergGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPrRELLEQWAEELRRFLGDPL 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 266 RIFIVDKSSDPlpdvctsntVAIMSYeQMVLKHDILKK--EKYRTIIFDESHMLkdGKARRTKVATDLSkvALHVILLSG 343
Cdd:COG1061 156 AGGGKKDSDAP---------ITVATY-QSLARRAHLDElgDRFGLVIIDEAHHA--GAPSYRRILEAFP--AAYRLGLTA 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 344 TPALS--RPSELFTQIRLIdhklftnfHEFAIRycdgkqgrfcfEAkgctnseelaaimfkrlmirrLKADVLKdlpekr 421
Cdd:COG1061 222 TPFRSdgREILLFLFDGIV--------YEYSLK-----------EA---------------------IEDGYLA------ 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 422 rEVVYVsgptidARMDDLQKARADYEKVNSMERKHesllefysltgIVKAAAVCEHILENYFYPDAPPRKVLIFAHHQIV 501
Cdd:COG1061 256 -PPEYY------GIRVDLTDERAEYDALSERLREA-----------LAADAERKDKILRELLREHPDDRKTLVFCSSVDH 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 502 LDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDnIRVaVLSITAAGVGITLTAASVVVFAEIHFNPGYLVQAEDR 581
Cdd:COG1061 318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGE-LRI-LVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395

                ...
gi 25148958 582 AHR 584
Cdd:COG1061 396 GLR 398
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
196-408 7.45e-13

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 68.65  E-value: 7.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALE-RDGRI-------LLADEMGLGKSVQALTIAryykadWPLL--------------IVCPASVKGAW 253
Cdd:cd18067   1 LRPHQREGVKFLYRcVTGRRirgshgcIMADEMGLGKTLQCITLM------WTLLrqspqckpeidkaiVVSPSSLVKNW 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 254 KKQLNTFFPIIHRIFIVDKSSDPLPDVCT-----------SNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKA 322
Cdd:cd18067  75 ANELGKWLGGRLQPLAIDGGSKKEIDRKLvqwasqqgrrvSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 323 rRTKVATDLSKVALHVIlLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRY---------CDGKQGRfcfEAKGCTNS 393
Cdd:cd18067 155 -QTYQALDSLNTQRRVL-LSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADASEKE---RQLGEEKL 229
                       250
                ....*....|....*
gi 25148958 394 EELAAIMfKRLMIRR 408
Cdd:cd18067 230 QELISIV-NRCIIRR 243
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
196-377 1.24e-12

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: 67.08  E-value: 1.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV---IFALERDGRILLADEMGLGKSVQALT-IARYYK---ADWPLLIVCPASVKGAWKKQLNTFFPiihRIF 268
Cdd:cd17994   1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVfLYSLYKeghSKGPFLVSAPLSTIINWEREFEMWAP---DFY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 269 IVDKSSDplpdvctsnTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLsKVAlHVILLSGTPALS 348
Cdd:cd17994  78 VVTYVGD---------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSY-KIG-YKLLLTGTPLQN 146
                       170       180
                ....*....|....*....|....*....
gi 25148958 349 RPSELFTQIRLIDHKLFTNFHEFAIRYCD 377
Cdd:cd17994 147 NLEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
196-410 1.76e-12

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: 67.41  E-value: 1.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV--IFALERDG-RILLADEMGLGKSVQAL-TIARYYKAD-W-PLLIVCPASVKGAWKKQLNTFFPIIHRIFI 269
Cdd:cd18009   4 MRPYQLEGMewLRMLWENGiNGILADEMGLGKTIQTIaLLAHLRERGvWgPFLVIAPLSTLPNWVNEFARFTPSVPVLLY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 270 ---------VDKSSDPLPDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKvatDLSKVAL-HVI 339
Cdd:cd18009  84 hgtkeererLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQ---ELKTFNSdNRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 340 LLSGTPALSRPSELFTQIRLIDHKLFTNFHEFA----IRYCdgKQGRFCFEAKgctnSEELAAIMFKRL-------MIRR 408
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFEswfdFSSL--SDNAADISNL----SEEREQNIVHMLhailkpfLLRR 234

                ..
gi 25148958 409 LK 410
Cdd:cd18009 235 LK 236
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
199-380 3.20e-12

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: 66.95  E-value: 3.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEGVIFALE---RDGRILLADEMGLGKSVQALTIARY----YKADWPLLIVCPASVKGAWKKQLNTFFPIIHRIFIVD 271
Cdd:cd18054  24 YQLEGLNWLAHswcKNNSVILADEMGLGKTIQTISFLSYlfhqHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVVYIG 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 272 kssdplpDVCTSNTV----------AIMSYEQMVLKHDILKKEK-------YRTIIFDESHMLKDGKARRTKVATDLSkv 334
Cdd:cd18054 104 -------DLMSRNTIreyewihsqtKRLKFNALITTYEILLKDKtvlgsinWAFLGVDEAHRLKNDDSLLYKTLIDFK-- 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 25148958 335 ALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQ 380
Cdd:cd18054 175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRE 220
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
199-408 3.23e-12

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: 66.62  E-value: 3.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEGV---IFALERDGRILLADEMGLGKSVQALT-IARYYKA--DWPLLIVCPASVKGAWKKQLNTFFPI--------- 263
Cdd:cd18060   4 YQLEGVnwlLFNWYNRQNCILADEMGLGKTIQSIAfLQEVYNVgiHGPFLVIAPLSTITNWEREFNTWTEMntivyhgsl 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 264 -------IHRIFIVDKSSDPLPDVCTSNTVaIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDgkaRRTKVATDLSKVAL 336
Cdd:cd18060  84 asrqmiqQYEMYCKDSRGRLIPGAYKFDAL-ITTFEMILSDCPELREIEWRCVIIDEAHRLKN---RNCKLLDSLKHMDL 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25148958 337 -HVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQGRfcfeakgctNSEELAAIMfKRLMIRR 408
Cdd:cd18060 160 eHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEE---------QVQKLQAIL-KPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
196-377 3.94e-12

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: 66.63  E-value: 3.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV---IFALERDGRILLADEMGLGKSVQ-ALTIARYYK---ADWPLLIVCPASVKGAWKKQLNTFFPIIHRI- 267
Cdd:cd18056   1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQtAVFLYSLYKeghSKGPFLVSAPLSTIINWEREFEMWAPDMYVVt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 268 FIVDKSSDPL-----------------------PDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARR 324
Cdd:cd18056  81 YVGDKDSRAIirenefsfednairggkkasrmkKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 25148958 325 TKVATDLSkvALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCD 377
Cdd:cd18056 161 FRVLNGYS--LQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD 211
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
215-410 1.01e-11

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 65.47  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARYY----KADWPLLIVCPASVKGAWKKQLNTFFPIIHRIFIVDKSS---DPLPDVCTSN-TV 286
Cdd:cd18063  46 ILADEMGLGKTIQTIALITYLmehkRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAmrrSLVPQLRSGKfNV 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 287 AIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVaTDLSKVALHVILLSGTPALSRPSELFTQIRLIDHKLFT 366
Cdd:cd18063 126 LLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV-LNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFK 204
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25148958 367 NFHEFAIRYcdgkQGRFCFEAKGCTNSEELAAIMFKRL-------MIRRLK 410
Cdd:cd18063 205 SCSTFEQWF----NAPFAMTGERVDLNEEETILIIRRLhkvlrpfLLRRLK 251
HELICc smart00490
helicase superfamily c-terminal domain;
503-586 1.10e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 61.07  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958    503 DTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNirVAVLSITAAGVGITLTAASVVVFAEIHFNPGYLVQAEDRA 582
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 25148958    583 HRVG 586
Cdd:smart00490  79 GRAG 82
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
215-410 1.12e-11

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 65.04  E-value: 1.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARYYK----ADWPLLIVCPASVKGAWKKQLNTFFPIIHRI-FIVDKSSDP--LPDVCTSNT-- 285
Cdd:cd18065  38 ILADEMGLGKTLQTIALLGYLKhyrnIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVcLIGDKDARAafIRDVMMPGEwd 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 286 VAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKValHVILLSGTPALSRPSELFTQIRLIDHKLF 365
Cdd:cd18065 118 VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTT--NRLLLTGTPLQNNLHELWALLNFLLPDVF 195
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 25148958 366 TNFHEFairycdgkqgRFCFEAKGCTNSEELAA---IMFKRLMIRRLK 410
Cdd:cd18065 196 NSADDF----------DSWFDTKNCLGDQKLVErlhAVLKPFLLRRIK 233
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
196-367 1.66e-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: 64.80  E-value: 1.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVI-------------FALERDGRIL-------------------LADEMGLGKSVQALTIAryykADWPLLI 243
Cdd:cd18071   1 LLPHQKQALAwmvsrensqdlppFWEEAVGLFLntitnfsqkkrpelvrggiLADDMGLGKTLTTISLI----LANFTLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 244 VCPASVKGAWKKQLNTFFPIIHRIFIVDKSSDPLPDVCTSNT--VAIMSYEqmVLKHDI-------LKKEKYRTIIFDES 314
Cdd:cd18071  77 VCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLSKydIVLTTYN--TLASDFgakgdspLHTINWLRVVLDEG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 25148958 315 HMLKDGKARRTKVATDLSkvALHVILLSGTPALSRPSELFTQIRLIDHKLFTN 367
Cdd:cd18071 155 HQIRNPNAQQTKAVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSN 205
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
215-410 6.36e-11

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 63.14  E-value: 6.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARYY----KADWPLLIVCPASVKGAWKKQLNTFFPIIHRifiVDKSSDP------LPDVCTSN 284
Cdd:cd18062  46 ILADEMGLGKTIQTIALITYLmehkRINGPFLIIVPLSTLSNWVYEFDKWAPSVVK---VSYKGSPaarrafVPQLRSGK 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 285 -TVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVaTDLSKVALHVILLSGTPALSRPSELFTQIRLIDHK 363
Cdd:cd18062 123 fNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV-LNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPT 201
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 25148958 364 LFTNFHEFAIRYcdgkQGRFCFEAKGCTNSEELAAIMFKRL-------MIRRLK 410
Cdd:cd18062 202 IFKSCSTFEQWF----NAPFAMTGEKVDLNEEETILIIRRLhkvlrpfLLRRLK 251
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
196-407 8.45e-11

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: 63.13  E-value: 8.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGriLLADEMGLGKSVQAL--------TIARYYKADWPL---------------------LIVCP 246
Cdd:cd18070   1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLalillhprPDNDLDAADDDSdemvccpdclvaetpvsskatLIVCP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 247 ASVKGAWKKQLNTFFPIIHRIFI------VDKSSDPLPD--------VCTSNTVAIMSYEQMVLKHD-----ILKKEKYR 307
Cdd:cd18070  79 SAILAQWLDEINRHVPSSLKVLTyqgvkkDGALASPAPEilaeydivVTTYDVLRTELHYAEANRSNrrrrrQKRYEAPP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 308 T---------IIFDESHMLKDGKARRTKVATDLSKValHVILLSGTPALSRPSELFTQIRLIDHKLFtnfhefairyCDG 378
Cdd:cd18070 159 SplvlvewwrVCLDEAQMVESSTSKAAEMARRLPRV--NRWCVSGTPIQRGLDDLFGLLSFLGVEPF----------CDS 226
                       250       260       270
                ....*....|....*....|....*....|
gi 25148958 379 K-QGRFCFEAKGCTNSEELAAIMFKRLMIR 407
Cdd:cd18070 227 DwWARVLIRPQGRNKAREPLAALLKELLWR 256
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
199-408 3.54e-10

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: 60.43  E-value: 3.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEGV---IFALERDGRILLADEMGLGKSVQALTIAR--YYKA-DWPLLIVCPASVKGAWKKQLNTFFPIIHRIFIVDK 272
Cdd:cd18059   4 YQLEGVnwlLFNWYNTRNCILADEMGLGKTIQSITFLYeiYLKGiHGPFLVIAPLSTIPNWEREFRTWTELNVVVYHGSQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 273 SS------------DPLPDVCTSNT---VAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDgkaRRTKVATDLSKVAL- 336
Cdd:cd18059  84 ASrrtiqlyemyfkDPQGRVIKGSYkfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKN---RNCKLLEGLKMMDLe 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25148958 337 HVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQGRfcfeakgctNSEELAAIMfKRLMIRR 408
Cdd:cd18059 161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEE---------QVQKLQAIL-KPMMLRR 222
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
215-380 1.02e-09

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: 59.29  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARY----YKADWPLLIVCPASVKGAWKKQLNTFFPIIHRIFIvdkssdpLPDVCTSNTVAI-- 288
Cdd:cd18053  43 ILADEMGLGKTIQTISFLNYlfheHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVVY-------LGDINSRNMIRThe 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 289 --------MSYEQMVLKHDILKKEK-------YRTIIFDESHMLKDGKARRTKVATDLSkvALHVILLSGTPALSRPSEL 353
Cdd:cd18053 116 wmhpqtkrLKFNILLTTYEILLKDKsflgglnWAFIGVDEAHRLKNDDSLLYKTLIDFK--SNHRLLITGTPLQNSLKEL 193
                       170       180
                ....*....|....*....|....*..
gi 25148958 354 FTQIRLIDHKLFTNFHEFAIRYCDGKQ 380
Cdd:cd18053 194 WSLLHFIMPEKFSSWEDFEEEHGKGRE 220
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
196-377 1.10e-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: 59.31  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV---IFALERDGRILLADEMGLGKSVQALT-IARYYK---ADWPLLIVCPASVKGAWKKQLNTFFPIIHRI- 267
Cdd:cd18057   1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTIVfLYSLYKeghSKGPYLVSAPLSTIINWEREFEMWAPDFYVVt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 268 FIVDKSSDPL-----------------------PDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARR 324
Cdd:cd18057  81 YTGDKESRSVirenefsfednairsgkkvfrmkKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 25148958 325 TKVATdlSKVALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCD 377
Cdd:cd18057 161 FRVLN--SYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
199-371 8.73e-09

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: 56.21  E-value: 8.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEGV---IFALERDGRILLADEMGLGKSVQALTIARY----YKADWPLLIVCPASVKGAWKKQLNTFFPIIHRI-FIV 270
Cdd:cd17993   5 YQLTGLnwlAHSWCKGNNGILADEMGLGKTVQTISFLSYlfhsQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIvYLG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 271 DKSSDplpDVC------TSNT------VAIMSYEqMVLK-HDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSkvALH 337
Cdd:cd17993  85 DIKSR---DTIreyefyFSQTkklkfnVLLTTYE-IILKdKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFK--TNN 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 25148958 338 VILLSGTPALSRPSELFTQIRLIDHKLFTNFHEF 371
Cdd:cd17993 159 RLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF 192
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
199-377 1.03e-08

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: 56.17  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEGV---IFALERDGRILLADEMGLGKSVQALT-IARYYK---ADWPLLIVCPASVKGAWKKQLNTFFPIIHRI-FIV 270
Cdd:cd18055   4 YQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVfLYSLYKeghTKGPFLVSAPLSTIINWEREFQMWAPDFYVVtYTG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 271 DKSSDPL-----------------------PDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKV 327
Cdd:cd18055  84 DKDSRAIirenefsfddnavkggkkafkmkREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRV 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 25148958 328 ATDLSkvALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCD 377
Cdd:cd18055 164 LNGYK--IDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
199-408 2.49e-08

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: 55.01  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 199 YQKEGV---IFALERDGRILLADEMGLGKSVQALT-IARYYKA--DWPLLIVCPASVKGAWKKQLNTFFPI----IHRIF 268
Cdd:cd18061   4 YQLEGLnwlLFNWYNRRNCILADEMGLGKTIQSITfLYEILLTgiRGPFLIIAPLSTIANWEREFRTWTDLnvvvYHGSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 269 IVDKSSDPLPDVCTSN-----------TVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDgkaRRTKVATDLSKVAL- 336
Cdd:cd18061  84 ISRQMIQQYEMYFRDSqgriirgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKN---KNCKLLEGLKLMNLe 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25148958 337 HVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQGRfcfeakgctNSEELAAIMfKRLMIRR 408
Cdd:cd18061 161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEE---------QVQKLQAIL-KPMMLRR 222
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
196-315 5.14e-06

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: 46.53  E-value: 5.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGV--IFALERDGRILLADEMGLGKSVQALTIARYYKADwPLLIVCP-ASVKGAWKKQLNTFFPIIHRIFIVDK 272
Cdd:cd17926   1 LRPYQEEALeaWLAHKNNRRGILVLPTGSGKTLTALALIAYLKEL-RTLIVVPtDALLDQWKERFEDFLGDSSIGLIGGG 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25148958 273 SSDPLPD----VCTSNTVAIMSYEQMVLKHDilkkekYRTIIFDESH 315
Cdd:cd17926  80 KKKDFDDanvvVATYQSLSNLAEEEKDLFDQ------FGLLIVDEAH 120
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
196-408 5.76e-06

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: 48.25  E-value: 5.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIFALERDGRI----LLADEMGLGK--SVQALTIARYYKAD------------WPL------------LIVC 245
Cdd:cd18072   1 LLLHQKQALAWLLWRERQKprggILADDMGLGKtlTMIALILAQKNTQNrkeeekekalteWESkkdstlvpsagtLVVC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 246 PASVKGAWKKQLNTffpiihrifivdKSSDPLPDVCT-------SNTVAIMSYEQMVLKHDILKKE-------------- 304
Cdd:cd18072  81 PASLVHQWKNEVES------------RVASNKLRVCLyhgpnreRIGEVLRDYDIVITTYSLVAKEiptykeesrssplf 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 305 --KYRTIIFDESHMLKDGKARRTKVATDLSKVALHVilLSGTPALSRPSELFTQIRLIDhklFTNFHEFairycdgKQGR 382
Cdd:cd18072 149 riAWARIILDEAHNIKNPKVQASIAVCKLRAHARWA--LTGTPIQNNLLDMYSLLKFLR---CSPFDDL-------KVWK 216
                       250       260
                ....*....|....*....|....*.
gi 25148958 383 FCFEAKGCTNSEELAAIMfKRLMIRR 408
Cdd:cd18072 217 KQVDNKSRKGGERLNILT-KSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
196-408 1.29e-04

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: 44.11  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 196 LFPYQKEGVIF-----------ALERDGR-ILLADEMGLGKSVQALTIA-------RYYKADwPLLIVCPASVKGAWKKQ 256
Cdd:cd18068   1 LKPHQVDGVQFmwdccceslkkTKKSPGSgCILAHCMGLGKTLQVVTFLhtvllceKLENFS-RVLVVCPLNTVLNWLNE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 257 ------------------LNTFFPIIHRIFIVDKSSDPlPDVCtsntvaIMSYEQ---MVLKHDILKKEKYRT------- 308
Cdd:cd18068  80 fekwqeglkdeekievneLATYKRPQERSYKLQRWQEE-GGVM------IIGYDMyriLAQERNVKSREKLKEifnkalv 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 309 ------IIFDESHMLKDGKARRTKVATdlSKVALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQ-G 381
Cdd:cd18068 153 dpgpdfVVCDEGHILKNEASAVSKAMN--SIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQnG 230
                       250       260
                ....*....|....*....|....*..
gi 25148958 382 RfcfeakgCTNSEELAAimfkRLMIRR 408
Cdd:cd18068 231 Q-------CADSTLVDV----RVMKKR 246
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
215-344 2.05e-04

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 42.01  E-value: 2.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148958 215 LLADEMGLGKSVQALTIARYYKADWPL--LIVCP-ASVKGAWKKQLNTFFPIIHRIFIVDKSSDPLPDvcTSNT-----V 286
Cdd:cd00046   5 LITAPTGSGKTLAALLAALLLLLKKGKkvLVLVPtKALALQTAERLRELFGPGIRVAVLVGGSSAEER--EKNKlgdadI 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25148958 287 AIMSYEQ---MVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKVALH---VILLSGT 344
Cdd:cd00046  83 IIATPDMllnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKnaqVILLSAT 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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