|
Name |
Accession |
Description |
Interval |
E-value |
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
200-803 |
5.81e-130 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 403.84 E-value: 5.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 200 AMLHKLFENNVLDNVKDDSMQRQSSFIP-GMHIRLLDHQVQGLTWLKSRETVSKssasGGILADDMGLGKTIQMIALILS 278
Cdd:COG0553 208 LLELELLAEAAVDAFRLRRLREALESLPaGLKATLRPYQLEGAAWLLFLRRLGL----GGLLADDMGLGKTIQALALLLE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 279 HplpKKKHSIKSTLVVAPLSLIKQWESEVQT-KSKLTAIVYHGAS-RYKLLKVIHEYDVVITTYQILVSEwvshnttgtd 356
Cdd:COG0553 284 L---KERGLARPVLIVAPTSLVGNWQRELAKfAPGLRVLVLDGTReRAKGANPFEDADLVITSYGLLRRD---------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 357 gkspteaksyekkKPSLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLhiNP-- 434
Cdd:COG0553 351 -------------IELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFL--NPgl 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 435 FNDQSVWKDQISLPLCQGEENLVfKRLRMLLSVIMLRRTKTLLeanagkdgtggALKLSKRLVYKVICKFEESERDFYSN 514
Cdd:COG0553 416 LGSLKAFRERFARPIEKGDEEAL-ERLRRLLRPFLLRRTKEDV-----------LKDLPEKTEETLYVELTPEQRALYEA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 515 LARNMERtmsnFVNSGKLGKNYTNILCLLLRLRQACNHPQslnfQFEQDVDAFNALDGaantnKLasdqdvDDLANLLET 594
Cdd:COG0553 484 VLEYLRR----ELEGAEGIRRRGLILAALTRLRQICSHPA----LLLEEGAELSGRSA-----KL------EALLELLEE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 595 VeigsrkksfcticmaelppdfhekkckdcsrnfkeLDKGiqdpndktlyksskireilkilsldeqeeddtvrglRKTI 674
Cdd:COG0553 545 L-----------------------------------LAEG------------------------------------EKVL 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 675 IFSQFTTFLDIIDLHLRKAGIGFVRYDGRMNNRAREKSLDLLRSDSGTQVLLCSLKCGALGLNLTCASRVILCDVWWNPA 754
Cdd:COG0553 554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPA 633
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 19111970 755 IEEQAIDRVHRIGQRRDVLVYKLVVENTIEEKIVELQNLKRDLAKQALG 803
Cdd:COG0553 634 VEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
233-472 |
3.89e-102 |
|
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: 315.77 E-value: 3.89e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRetvskssasGGILADDMGLGKTIQMIALILSHPLPKKKHSI---------------KSTLVVAPL 297
Cdd:cd18008 1 LLPYQKQGLAWMLPR---------GGILADEMGLGKTIQALALILATRPQDPKIPEeleenssdpkklylsKTTLIVVPL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 298 SLIKQWESEVQTKSK---LTAIVYHGASRYKLLKVIHEYDVVITTYQILVSEWvshnttgTDGKSPTEAKSYEKKKPSLF 374
Cdd:cd18008 72 SLLSQWKDEIEKHTKpgsLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEF-------PKNKKGGGRDSKEKEASPLH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 375 AFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLcQGEE 454
Cdd:cd18008 145 RIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF-SKND 223
|
250
....*....|....*...
gi 19111970 455 NLVFKRLRMLLSVIMLRR 472
Cdd:cd18008 224 RKALERLQALLKPILLRR 241
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
236-556 |
5.80e-77 |
|
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: 251.06 E-value: 5.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWLKSRETVSKSsasGGILADDMGLGKTIQMIALILsHPLPKKKHSIKSTLVVAPLSLIKQWESEVQT---KSK 312
Cdd:pfam00176 1 YQIEGVNWMLSLENNLGR---GGILADEMGLGKTLQTISLLL-YLKHVDKNWGGPTLIVVPLSLLHNWMNEFERwvsPPA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 313 LTAIVYHGASRYKLL-----KVIHEYDVVITTYQILVSEWVSHNTTGtdgkspteaksyekkkpslfafyWWRIILDEAH 387
Cdd:pfam00176 77 LRVVVLHGNKRPQERwkndpNFLADFDVVITTYETLRKHKELLKKVH-----------------------WHRIVLDEGH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 388 TIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQGEENLVFKRLRMLLSV 467
Cdd:pfam00176 134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSRLHKLLKP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 468 IMLRRTKTLLEANagkdgtggalkLSKRLVYKVICKFEESERDFYSN--LARNMertmsNFVNSGKLG-KNYTNILCLLL 544
Cdd:pfam00176 214 FLLRRTKKDVEKS-----------LPPKVEYILFCRLSKLQRKLYQTflLKKDL-----NAIKTGEGGrEIKASLLNILM 277
|
330
....*....|..
gi 19111970 545 RLRQACNHPQSL 556
Cdd:pfam00176 278 RLRKICNHPGLI 289
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
233-472 |
4.87e-67 |
|
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: 222.74 E-value: 4.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSREtvsKSSASGGILADDMGLGKTIQMIALILSHPLP------KKKHSI--------------KSTL 292
Cdd:cd18072 1 LLLHQKQALAWLLWRE---RQKPRGGILADDMGLGKTLTMIALILAQKNTqnrkeeEKEKALteweskkdstlvpsAGTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 293 VVAPLSLIKQWESEVQTK---SKLTAIVYHGASRYKLLKVIHEYDVVITTYQILVSEWVSHNTTGTdgKSPteaksyekk 369
Cdd:cd18072 78 VVCPASLVHQWKNEVESRvasNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEESR--SSP--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 370 kpsLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPL 449
Cdd:cd18072 147 ---LFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKS 223
|
250 260
....*....|....*....|...
gi 19111970 450 CQGEEnlvfkRLRMLLSVIMLRR 472
Cdd:cd18072 224 RKGGE-----RLNILTKSLLLRR 241
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
233-472 |
1.36e-58 |
|
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: 199.62 E-value: 1.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRE------------------TVSKSSAS-------GGILADDMGLGKTIQMIALILSHPlpkkkhs 287
Cdd:cd18071 1 LLPHQKQALAWMVSREnsqdlppfweeavglflnTITNFSQKkrpelvrGGILADDMGLGKTLTTISLILANF------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 288 iksTLVVAPLSLIKQWESEVQTKSK---LTAIVYHGASRYKLLKVIHEYDVVITTYQILVSEWvshnttGTDGKSPteak 364
Cdd:cd18071 74 ---TLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGGERNRDPKLLSKYDIVLTTYNTLASDF------GAKGDSP---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 365 syekkkpsLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQ 444
Cdd:cd18071 141 --------LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRL 212
|
250 260
....*....|....*....|....*...
gi 19111970 445 ISLPLCQGEENlVFKRLRMLLSVIMLRR 472
Cdd:cd18071 213 IQRPLTMGDPT-GLKRLQVLMKQITLRR 239
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
233-471 |
7.97e-56 |
|
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: 192.94 E-value: 7.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKsretvskssASGGILADDMGLGKTIQMIALILSHPLPKKKH-----------------------SIK 289
Cdd:cd18070 1 LLPYQRRAVNWML---------VPGGILADEMGLGKTVEVLALILLHPRPDNDLdaadddsdemvccpdclvaetpvSSK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 290 STLVVAPLSLIKQWESEVQ--TKSKLTAIVYHGASRYKLLK--VIH---EYDVVITTYQILVSEwVSHNTTGTDGKSPTE 362
Cdd:cd18070 72 ATLIVCPSAILAQWLDEINrhVPSSLKVLTYQGVKKDGALAspAPEilaEYDIVVTTYDVLRTE-LHYAEANRSNRRRRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 363 AKSYEKKKPSLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFnDQSVWK 442
Cdd:cd18070 151 QKRYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPF-CDSDWW 229
|
250 260
....*....|....*....|....*....
gi 19111970 443 DQIsLPLCQGEENLVfKRLRMLLSVIMLR 471
Cdd:cd18070 230 ARV-LIRPQGRNKAR-EPLAALLKELLWR 256
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
646-778 |
3.04e-52 |
|
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: 178.05 E-value: 3.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 646 SSKIREILKILSLDEQEEDdtvrglrKTIIFSQFTTFLDIIDLHLRKAGIGFVRYDGRMNNRAREKSLDLLRSDSGTQVL 725
Cdd:cd18793 10 SGKLEALLELLEELREPGE-------KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVF 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 19111970 726 LCSLKCGALGLNLTCASRVILCDVWWNPAIEEQAIDRVHRIGQRRDVLVYKLV 778
Cdd:cd18793 83 LLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
233-474 |
6.59e-51 |
|
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: 177.76 E-value: 6.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRETvsksSASGGILADDMGLGKTIQMIALILSHplpKKKHSIKSTLVVAPLSLIKQWESEVQT-KS 311
Cdd:cd18012 5 LRPYQKEGFNWLSFLRH----YGLGGILADDMGLGKTLQTLALLLSR---KEEGRKGPSLVVAPTSLIYNWEEEAAKfAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHGASRYKL-LKVIHEYDVVITTYQILVSEwvshnttgtdgkspteAKSYEKKKpslfafyWWRIILDEAHTIK 390
Cdd:cd18012 78 ELKVLVIHGTKRKREkLRALEDYDLVITSYGLLRRD----------------IELLKEVK-------FHYLVLDEAQNIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 391 NKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLhiNP--FNDQSVWKDQISLPLCQGEENLVFKRLRMLLSVI 468
Cdd:cd18012 135 NPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFL--NPglLGSYKRFKKRFAKPIEKDGDEEALEELKKLISPF 212
|
....*.
gi 19111970 469 MLRRTK 474
Cdd:cd18012 213 ILRRLK 218
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
233-431 |
3.12e-49 |
|
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: 171.59 E-value: 3.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSREtvskSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KS 311
Cdd:cd17919 1 LRPYQLEGLNFLLELY----ENGPGGILADEMGLGKTLQAIAFLAY--LLKEGKERGPVLVVCPLSVLENWEREFEKwTP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHGASR----YKLLKVIHEYDVVITTYQILvsewvshnttgtdgkspteaksyEKKKPSLFAFYWWRIILDEAH 387
Cdd:cd17919 75 DLRVVVYHGSQReraqIRAKEKLDKFDVVLTTYETL-----------------------RRDKASLRKFRWDLVVVDEAH 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19111970 388 TIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLH 431
Cdd:cd17919 132 RLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLD 175
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
219-789 |
2.01e-47 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 182.69 E-value: 2.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 219 MQRQSSFIPGmhiRLLDHQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLS 298
Cdd:PLN03142 159 LLVQPSCIKG---KMRDYQLAGLNWLIRL----YENGINGILADEMGLGKTLQTISLLGY--LHEYRGITGPHMVVAPKS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 299 LIKQWESEVQTKSK-LTAIVYHG------ASRYKLLkVIHEYDVVITTYQILVsewvshnttgtdgkspteaksyeKKKP 371
Cdd:PLN03142 230 TLGNWMNEIRRFCPvLRAVKFHGnpeeraHQREELL-VAGKFDVCVTSFEMAI-----------------------KEKT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 372 SLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKD--QISlpl 449
Cdd:PLN03142 286 ALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEwfQIS--- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 450 CQGEENLVFKRLRMLLSVIMLRRTKTLLEANagkdgtggaLKLSKRLVYKVicKFEESERDFYSN-LARNMErtmsnFVN 528
Cdd:PLN03142 363 GENDQQEVVQQLHKVLRPFLLRRLKSDVEKG---------LPPKKETILKV--GMSQMQKQYYKAlLQKDLD-----VVN 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 529 SGKLGKNYTNIlclLLRLRQACNHPQslnfqfeqdvdafnaldgaantnklasdqdvddlanLLETVEIGsrkksfctic 608
Cdd:PLN03142 427 AGGERKRLLNI---AMQLRKCCNHPY------------------------------------LFQGAEPG---------- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 609 maelPPDFHEKKCKDCSRNFKELDKgiqdpndktlyksskireILKILsldeQEEDDTVrglrktIIFSQFTTFLDIIDL 688
Cdd:PLN03142 458 ----PPYTTGEHLVENSGKMVLLDK------------------LLPKL----KERDSRV------LIFSQMTRLLDILED 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 689 HLRKAGIGFVRYDGRMNNRAREKSLDLL-RSDSGTQVLLCSLKCGALGLNLTCASRVILCDVWWNPAIEEQAIDRVHRIG 767
Cdd:PLN03142 506 YLMYRGYQYCRIDGNTGGEDRDASIDAFnKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIG 585
|
570 580
....*....|....*....|..
gi 19111970 768 QRRDVLVYKLVVENTIEEKIVE 789
Cdd:PLN03142 586 QKKEVQVFRFCTEYTIEEKVIE 607
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
233-430 |
1.78e-41 |
|
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: 151.76 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRETVSKssasGGILADDMGLGKTIQMIALILShpLPKKKHsIKSTLVVAPLSLIKQWESEVQTKS- 311
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGK----GGILADDMGLGKTVQICAFLSG--MFDSGL-IKSVLVVMPTSLIPHWVKEFAKWTp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHGASR----YKLLKVIHEYDVVITTYQILVSEWVSHNTTGTDGkspteaksyekkkpslfaFYWWRIILDEAH 387
Cdd:cd18001 74 GLRVKVFHGTSKkereRNLERIQRGGGVLLTTYGMVLSNTEQLSADDHDE------------------FKWDYVILDEGH 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19111970 388 TIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFL 430
Cdd:cd18001 136 KIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
233-472 |
6.49e-39 |
|
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: 143.93 E-value: 6.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRETVSKSSasggILADDMGLGKTIQMIALiLSHPLpkKKHSIKST-LVVAPLSLIKQWESEVQTKS 311
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNC----ILADEMGLGKTIQSIAF-LEHLY--QVEGIRGPfLVIAPLSTIPNWQREFETWT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHG--ASR---------YKLLKV-----IHEYDVVITTYQILVSEWvshnttgtdgkspteaksyekkkPSLFA 375
Cdd:cd17995 74 DMNVVVYHGsgESRqiiqqyemyFKDAQGrkkkgVYKFDVLITTYEMVIADA-----------------------EELRK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 376 FYWWRIILDEAHTIKNKSSKSalaccaLQGINRWC------LTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQislpL 449
Cdd:cd17995 131 IPWRVVVVDEAHRLKNRNSKL------LQGLKKLTlehkllLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEE----F 200
|
250 260
....*....|....*....|...
gi 19111970 450 CQGEENLVFKRLRMLLSVIMLRR 472
Cdd:cd17995 201 GDLKTAEQVEKLQALLKPYMLRR 223
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
232-474 |
5.53e-37 |
|
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: 138.61 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 232 RLLDHQVQGLTWLKS--RETVSkssasgGILADDMGLGKTIQMIALI--LSH----PLPkkkHsikstLVVAPLSLIKQW 303
Cdd:cd17997 3 TMRDYQIRGLNWLISlfENGIN------GILADEMGLGKTLQTISLLgyLKHykniNGP---H-----LIIVPKSTLDNW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 304 ESEVQT-KSKLTAIVYHGA--SRYKLLK---VIHEYDVVITTYQILVSEwvshnttgtdgkspteaKSYEKKkpslfaFY 377
Cdd:cd17997 69 MREFKRwCPSLRVVVLIGDkeERADIIRdvlLPGKFDVCITSYEMVIKE-----------------KTVLKK------FN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 378 WWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQGEENLV 457
Cdd:cd17997 126 WRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEV 205
|
250
....*....|....*..
gi 19111970 458 FKRLRMLLSVIMLRRTK 474
Cdd:cd17997 206 VQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
233-472 |
3.44e-35 |
|
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: 134.04 E-value: 3.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRETVSKssasGGILADDMGLGKTIQMIALILS--------------HPLPKKKHSIKST----LVV 294
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGR----GGILGDDMGLGKTVQVIAFLAAvlgktgtrrdrennRPRFKKKPPASSAkkpvLIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 295 APLSLIKQWESEVQTKSKLTAIVYHG-------ASRYKLLKviheYDVVITTYQILVSEwvshnttgtdgkspteaksye 367
Cdd:cd18005 77 APLSVLYNWKDELDTWGHFEVGVYHGsrkddelEGRLKAGR----LEVVVTTYDTLRRC--------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 368 kkKPSLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISL 447
Cdd:cd18005 132 --IDSLNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSE 209
|
250 260 270
....*....|....*....|....*....|....*.
gi 19111970 448 PLCQG------EENLVFKRLRM-----LLSVIMLRR 472
Cdd:cd18005 210 PIKRGqrhtatARELRLGRKRKqelavKLSKFFLRR 245
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
233-474 |
3.36e-34 |
|
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: 130.95 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KS 311
Cdd:cd17996 4 LKEYQLKGLQWMVSL----YNNNLNGILADEMGLGKTIQTISLITY--LMEKKKNNGPYLVIVPLSTLSNWVSEFEKwAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHG--ASRYKLLKVIH--EYDVVITTYQILVsewvshnttgtdgkspteaksyeKKKPSLFAFYWWRIILDEAH 387
Cdd:cd17996 78 SVSKIVYKGtpDVRKKLQSQIRagKFNVLLTTYEYII-----------------------KDKPLLSKIKWKYMIIDEGH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 388 TIKNKSSK-SALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLP-----------LCQGEEN 455
Cdd:cd17996 135 RMKNAQSKlTQTLNTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPfantgeqvkieLNEEETL 214
|
250
....*....|....*....
gi 19111970 456 LVFKRLRMLLSVIMLRRTK 474
Cdd:cd17996 215 LIIRRLHKVLRPFLLRRLK 233
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
233-451 |
5.21e-31 |
|
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: 121.69 E-value: 5.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRETVSKSsasgGILADDMGLGKTIQMIALI-LSHPLPKKKHSIKS--TLVVAPLSLIKQWESEVQT 309
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLH----GILCDDMGLGKTLQTLCILaSDHHKRANSFNSENlpSLVVCPPTLVGHWVAEIKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 310 ---KSKLTAIVYHGAS--RYKLLKVIHEYDVVITTYQILVSEwvshnttgtdgkspteaksYEkkkpSLFAFYWWRIILD 384
Cdd:cd17999 77 yfpNAFLKPLAYVGPPqeRRRLREQGEKHNVIVASYDVLRND-------------------IE----VLTKIEWNYCVLD 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111970 385 EAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQ 451
Cdd:cd17999 134 EGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILA 200
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
233-431 |
6.27e-31 |
|
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: 120.12 E-value: 6.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTW---LKSRETvskssasGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT 309
Cdd:cd18000 1 LFKYQQTGVQWlweLHCQRV-------GGILGDEMGLGKTIQIIAFLAA--LHHSKLGLGPSLIVCPATVLKQWVKEFHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 310 -KSKLTAIVYH------GASRYKLL---------KVIHEYDVVITTYQILvsewvshnttgtdgkspteaksyEKKKPSL 373
Cdd:cd18000 72 wWPPFRVVVLHssgsgtGSEEKLGSierksqlirKVVGDGGILITTYEGF-----------------------RKHKDLL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19111970 374 FAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLH 431
Cdd:cd18000 129 LNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVF 186
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
233-474 |
4.98e-30 |
|
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: 119.03 E-value: 4.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALIlshPLPKKKHSIKSTLVVAPLSLIKQWESEVQTKS- 311
Cdd:cd18009 4 MRPYQLEGMEWLRML----WENGINGILADEMGLGKTIQTIALL---AHLRERGVWGPFLVIAPLSTLPNWVNEFARFTp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHGASRYKllkviheydvvittyQILVSEWVSHNTTGtdGKSPTEAKSYE---KKKPSLFAFYWWRIILDEAHT 388
Cdd:cd18009 77 SVPVLLYHGTKEER---------------ERLRKKIMKREGTL--QDFPVVVTSYEiamRDRKALQHYAWKYLIVDEGHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 389 IKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSV---WKDQISLPLCQGEENL--------V 457
Cdd:cd18009 140 LKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSfesWFDFSSLSDNAADISNlseereqnI 219
|
250
....*....|....*..
gi 19111970 458 FKRLRMLLSVIMLRRTK 474
Cdd:cd18009 220 VHMLHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
233-435 |
2.99e-29 |
|
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: 115.18 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLksreTVSKSSASGGILADDMGLGKTIQMIALiLSHPLPKKKHSikSTLVVAPLSLIKQWESEVQT-KS 311
Cdd:cd17998 1 LKDYQLIGLNWL----NLLYQKKLSGILADEMGLGKTIQVIAF-LAYLKEIGIPG--PHLVVVPSSTLDNWLREFKRwCP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHGAS------RYKLLKVIHEYDVVITTYQIlvsewvshnTTGTDgksptEAKSYEKKKPSLFAFYwwriilDE 385
Cdd:cd17998 74 SLKVEPYYGSQeerkhlRYDILKGLEDFDVIVTTYNL---------ATSNP-----DDRSFFKRLKLNYVVY------DE 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19111970 386 AHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPF 435
Cdd:cd17998 134 GHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
233-472 |
3.05e-29 |
|
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: 116.30 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLksreTVSKSSASGGILADDMGLGKTIQMIALiLSHpLPKKKHSIKSTLVVAPLSLIKQWESEVQTKSK 312
Cdd:cd18003 1 LREYQHIGLDWL----ATLYEKNLNGILADEMGLGKTIQTIAL-LAH-LACEKGNWGPHLIVVPTSVMLNWEMEFKRWCP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 313 -LTAIVYHGASRYKLLK--------VIHeydVVITTYQILVSEwvshnttgtdgkspteAKSYEKKKpslfafyWWRIIL 383
Cdd:cd18003 75 gFKILTYYGSAKERKLKrqgwmkpnSFH---VCITSYQLVVQD----------------HQVFKRKK-------WKYLIL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 384 DEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPL---CQGEENL---V 457
Cdd:cd18003 129 DEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLtamSEGSQEEneeL 208
|
250
....*....|....*
gi 19111970 458 FKRLRMLLSVIMLRR 472
Cdd:cd18003 209 VRRLHKVLRPFLLRR 223
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
236-472 |
3.76e-29 |
|
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: 116.62 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWLKSRETVSKSSASGG-ILADDMGLGKTIQMIALI---LSHPlPKKKHSIKSTLVVAPLSLIKQWESEVQT-- 309
Cdd:cd18004 4 HQREGVQFLYDCLTGRRGYGGGGaILADEMGLGKTLQAIALVwtlLKQG-PYGKPTAKKALIVCPSSLVGNWKAEFDKwl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 310 -KSKLTAIVYHGASRYKLLKVIHE-----YDVVITTYQILVSewvsHNttgtdgkspteAKSYEKKKPSLfafywwrIIL 383
Cdd:cd18004 83 gLRRIKVVTADGNAKDVKASLDFFssastYPVLIISYETLRR----HA-----------EKLSKKISIDL-------LIC 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 384 DEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFlhINP--FNDQSVWKDQISLP-LCQGEEN----- 455
Cdd:cd18004 141 DEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDF--VNPgiLGSLASFRKVFEEPiLRSRDPDaseed 218
|
250 260
....*....|....*....|..
gi 19111970 456 -----LVFKRLRMLLSVIMLRR 472
Cdd:cd18004 219 kelgaERSQELSELTSRFILRR 240
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
233-472 |
1.06e-27 |
|
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: 111.67 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSRETVSKSSasggILADDMGLGKTIQMIALiLSHPLPKKKHSikSTLVVAPLSLIKQWESEVQTKSK 312
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNC----ILADEMGLGKTIQSITF-LSEIFLMGIRG--PFLIIAPLSTITNWEREFRTWTE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 313 LTAIVYHGA--SRYKLLKV--------------IHEYDVVITTYQILVSEWvshnttgtdgkspteaksyekkkPSLFAF 376
Cdd:cd18058 74 MNAIVYHGSqiSRQMIQQYemyyrdeqgnplsgIFKFQVVITTFEMILADC-----------------------PELKKI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 377 YWWRIILDEAHTIKNKSSK--SALACCALQgiNRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISlpLCQGEE 454
Cdd:cd18058 131 NWSCVIIDEAHRLKNRNCKllEGLKLMALE--HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG--DLKTEE 206
|
250
....*....|....*...
gi 19111970 455 NLvfKRLRMLLSVIMLRR 472
Cdd:cd18058 207 QV--KKLQSILKPMMLRR 222
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
218-472 |
2.54e-27 |
|
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: 111.25 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 218 SMQRQSSFIPGMHIRLLDHQVQGLTWLKSRETVSKSSasggILADDMGLGKTIQMIALI--LSHplpkkKHSIKST-LVV 294
Cdd:cd18054 6 ALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSV----ILADEMGLGKTIQTISFLsyLFH-----QHQLYGPfLLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 295 APLSLIKQWESEVQT-KSKLTAIVYHG--ASRykllKVIHEYD------------VVITTYQILVsewvshnttgtdgks 359
Cdd:cd18054 77 VPLSTLTSWQREFEIwAPEINVVVYIGdlMSR----NTIREYEwihsqtkrlkfnALITTYEILL--------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 360 pteaksyeKKKPSLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQS 439
Cdd:cd18054 138 --------KDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWE 209
|
250 260 270
....*....|....*....|....*....|...
gi 19111970 440 VWKDQISlplcQGEENlVFKRLRMLLSVIMLRR 472
Cdd:cd18054 210 DFEEDHG----KGREN-GYQSLHKVLEPFLLRR 237
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
233-472 |
7.76e-27 |
|
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: 108.98 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLksreTVSKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KS 311
Cdd:cd17993 2 LRDYQLTGLNWL----AHSWCKGNNGILADEMGLGKTVQTISFLSY--LFHSQQQYGPFLVVVPLSTMPAWQREFAKwAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHG--ASRykllKVIHEYD------------VVITTYQILVsewvshnttgtdgkspteaksyeKKKPSLFAFY 377
Cdd:cd17993 76 DMNVIVYLGdiKSR----DTIREYEfyfsqtkklkfnVLLTTYEIIL-----------------------KDKAFLGSIK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 378 WWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFndqSVWKDqisLPLCQGEEN-L 456
Cdd:cd17993 129 WQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKF---DIWEE---FEEEHDEEQeK 202
|
250
....*....|....*.
gi 19111970 457 VFKRLRMLLSVIMLRR 472
Cdd:cd17993 203 GIADLHKELEPFILRR 218
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
232-478 |
1.05e-26 |
|
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: 109.76 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 232 RLLDHQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALI--LSH----PLPKkkhsikstLVVAPLSLIKQWES 305
Cdd:cd18064 15 KLRDYQVRGLNWLISL----YENGINGILADEMGLGKTLQTISLLgyMKHyrniPGPH--------MVLVPKSTLHNWMA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 306 EVQ---TKSKLTAIVYHGASRYKLLKVI---HEYDVVITTYQILVSEwvshnttgtdgkspteaKSYEKKkpslfaFYWW 379
Cdd:cd18064 83 EFKrwvPTLRAVCLIGDKDQRAAFVRDVllpGEWDVCVTSYEMLIKE-----------------KSVFKK------FNWR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 380 RIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQGEENLVfK 459
Cdd:cd18064 140 YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLV-E 218
|
250
....*....|....*....
gi 19111970 460 RLRMLLSVIMLRRTKTLLE 478
Cdd:cd18064 219 RLHMVLRPFLLRRIKADVE 237
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
224-474 |
6.27e-26 |
|
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: 107.03 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 224 SFIPGMHIRllDHQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALI--LSH----PLPKkkhsikstLVVAPL 297
Cdd:cd18065 9 SYVKGGTLR--DYQVRGLNWMISL----YENGVNGILADEMGLGKTLQTIALLgyLKHyrniPGPH--------MVLVPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 298 SLIKQWESEVQT-KSKLTAIVYHG-----ASRYKLLKVIHEYDVVITTYQILVSEwvshnttgtdgkspteaKSYEKKkp 371
Cdd:cd18065 75 STLHNWMNEFKRwVPSLRAVCLIGdkdarAAFIRDVMMPGEWDVCVTSYEMVIKE-----------------KSVFKK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 372 slfaFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQ 451
Cdd:cd18065 136 ----FNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCL 211
|
250 260
....*....|....*....|...
gi 19111970 452 GEENLVfKRLRMLLSVIMLRRTK 474
Cdd:cd18065 212 GDQKLV-ERLHAVLKPFLLRRIK 233
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
236-472 |
1.35e-25 |
|
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: 105.60 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KSKLT 314
Cdd:cd18006 4 YQLEGVNWLLQC----RAEQHGCILGDEMGLGKTCQTISLLWY--LAGRLKLLGPFLVLCPLSVLDNWKEELNRfAPDLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 315 AIVYHGASRYKL-----LKVIHEYDVVITTYQILVSEwvshnttgtdgkspteaKSYEKKkpslfaFYWWRIILDEAHTI 389
Cdd:cd18006 78 VITYMGDKEKRLdlqqdIKSTNRFHVLLTTYEICLKD-----------------ASFLKS------FPWASLVVDEAHRL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 390 KNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVwKDQISLPLCQGEENLVFKRLRMLLSVIM 469
Cdd:cd18006 135 KNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKL-DDFIKAYSETDDESETVEELHLLLQPFL 213
|
...
gi 19111970 470 LRR 472
Cdd:cd18006 214 LRR 216
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
233-472 |
1.81e-25 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350818 [Multi-domain] Cd Length: 222 Bit Score: 105.52 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLksreTVSKSSASGGILADDMGLGKTIQMIALILShplpKKKHSIKST-LVVAPLSLIKQWESEVQTKS 311
Cdd:cd18060 1 LREYQLEGVNWL----LFNWYNRQNCILADEMGLGKTIQSIAFLQE----VYNVGIHGPfLVIAPLSTITNWEREFNTWT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHGA----------------SRYKLLKVIHEYDVVITTYQILVSEWvshnttgtdgkspteaksyekkkPSLFA 375
Cdd:cd18060 73 EMNTIVYHGSlasrqmiqqyemyckdSRGRLIPGAYKFDALITTFEMILSDC-----------------------PELRE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 376 FYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVW-KDQISLplcQGEE 454
Cdd:cd18060 130 IEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFlKDFGDL---KTEE 206
|
250
....*....|....*...
gi 19111970 455 NLvfKRLRMLLSVIMLRR 472
Cdd:cd18060 207 QV--QKLQAILKPMMLRR 222
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
233-472 |
8.80e-25 |
|
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: 103.74 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSretvSKSSASGGILADDMGLGKTIQMIALiLSHpLPKKKHSIKSTLVVAPLSLIKQWESEV-QTKS 311
Cdd:cd18002 1 LKEYQLKGLNWLAN----LYEQGINGILADEMGLGKTVQSIAV-LAH-LAEEHNIWGPFLVIAPASTLHNWQQEIsRFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHG--ASRYKLLKVIHE---------YDVVITTYQILVsewvshnttgtdgkspTEAKSYEKKKpslfafyWWR 380
Cdd:cd18002 75 QFKVLPYWGnpKDRKVLRKFWDRknlytrdapFHVVITSYQLVV----------------QDEKYFQRVK-------WQY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 381 IILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQGEENLV--- 457
Cdd:cd18002 132 MVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTgln 211
|
250
....*....|....*...
gi 19111970 458 ---FKRLRMLLSVIMLRR 472
Cdd:cd18002 212 ehqLKRLHMILKPFMLRR 229
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
231-436 |
1.39e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 102.18 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 231 IRLLDHQVQGLTWLKSREtvskssaSGGILADDMGLGKTIQMIALILSHplpKKKHSIKSTLVVAPL-SLIKQWESEVQT 309
Cdd:smart00487 7 EPLRPYQKEAIEALLSGL-------RDVILAAPTGSGKTLAALLPALEA---LKRGKGGRVLVLVPTrELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 310 KSKLTAI----VYHGASRYKLLKVIHE--YDVVITTYQILVsewvshnttgtdgkspteaksYEKKKPSLFAFYWWRIIL 383
Cdd:smart00487 77 LGPSLGLkvvgLYGGDSKREQLRKLESgkTDILVTTPGRLL---------------------DLLENDKLSLSNVDLVIL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19111970 384 DEAHTIKNKSSKSALACC---ALQGINRWCLTGTP---LQNNVDELYSLVKFLHINPFN 436
Cdd:smart00487 136 DEAHRLLDGGFGDQLEKLlklLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTP 194
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
233-472 |
1.82e-24 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350817 [Multi-domain] Cd Length: 222 Bit Score: 102.42 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLksreTVSKSSASGGILADDMGLGKTIQMIALILSHPLpKKKHSikSTLVVAPLSLIKQWESEVQTKSK 312
Cdd:cd18059 1 LREYQLEGVNWL----LFNWYNTRNCILADEMGLGKTIQSITFLYEIYL-KGIHG--PFLVIAPLSTIPNWEREFRTWTE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 313 LTAIVYHG--ASRY--------------KLLKVIHEYDVVITTYQILVSEWvshnttgtdgkspteaksyekkkPSLFAF 376
Cdd:cd18059 74 LNVVVYHGsqASRRtiqlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDC-----------------------PELRNI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 377 YWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISlpLCQGEENL 456
Cdd:cd18059 131 PWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG--DLKTEEQV 208
|
250
....*....|....*.
gi 19111970 457 vfKRLRMLLSVIMLRR 472
Cdd:cd18059 209 --QKLQAILKPMMLRR 222
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
233-472 |
4.94e-24 |
|
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: 100.21 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKsretVSKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KS 311
Cdd:cd17994 1 LHPYQLEGLNWLR----FSWAQGTDTILADEMGLGKTIQTIVFLYS--LYKEGHSKGPFLVSAPLSTIINWEREFEMwAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 312 KLTAIVYHGASrykllkviheydVVITTYQILVSEwvshnttgtdgkspteaksyekkKPSLFAFYWWRIILDEAHTIKN 391
Cdd:cd17994 75 DFYVVTYVGDH------------VLLTSYELISID-----------------------QAILGSIDWAVLVVDEAHRLKN 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 392 KSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISlpLCQGEENLvfKRLRMLLSVIMLR 471
Cdd:cd17994 120 NQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA--DISKEDQI--KKLHDLLGPHMLR 195
|
.
gi 19111970 472 R 472
Cdd:cd17994 196 R 196
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
647-767 |
1.39e-23 |
|
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: 96.13 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 647 SKIREILKILSLDEQEeddtvrglrKTIIFSQFTTFLDIiDLHLRKAGIGFVRYDGRMNNRAREKSLDLLRSDSgTQVLL 726
Cdd:pfam00271 1 EKLEALLELLKKERGG---------KVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK-IDVLV 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 19111970 727 CSlKCGALGLNLTCASRVILCDVWWNPAIEEQAIDRVHRIG 767
Cdd:pfam00271 70 AT-DVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
233-429 |
1.80e-23 |
|
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: 100.06 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSR--ETVSKSSASGG-ILADDMGLGKTIQMIALI---LSHPLPKKKhsiksTLVVAPLSLIKQWESE 306
Cdd:cd18007 1 LKPHQVEGVRFLWSNlvGTDVGSDEGGGcILAHTMGLGKTLQVITFLhtyLAAAPRRSR-----PLVLCPASTLYNWEDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 307 VQTKSKLTAIVYHGASRYKL-------LKVI----HEYDVVITTYQILVsewvshNTTGTDGKSPTEAKSYEK----KKP 371
Cdd:cd18007 76 FKKWLPPDLRPLLVLVSLSAskradarLRKInkwhKEGGVLLIGYELFR------NLASNATTDPRLKQEFIAalldPGP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19111970 372 SLfafywwrIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKF 429
Cdd:cd18007 150 DL-------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDF 200
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
233-472 |
2.09e-23 |
|
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: 99.31 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLksreTVSKSSASGGILADDMGLGKTIQMIALILSHPLPKKKHSIkstLVVAPLSLIKQWESEVQTKSK 312
Cdd:cd18061 1 LREYQLEGLNWL----LFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPF---LIIAPLSTIANWEREFRTWTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 313 LTAIVYHGA----------------SRYKLLKVIHEYDVVITTYQILVSEWvshnttgtdgkspteaksyekkkPSLFAF 376
Cdd:cd18061 74 LNVVVYHGSlisrqmiqqyemyfrdSQGRIIRGAYRFQAIITTFEMILGGC-----------------------PELNAI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 377 YWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISlpLCQGEENL 456
Cdd:cd18061 131 DWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG--DLKTEEQV 208
|
250
....*....|....*.
gi 19111970 457 vfKRLRMLLSVIMLRR 472
Cdd:cd18061 209 --QKLQAILKPMMLRR 222
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
218-443 |
5.64e-21 |
|
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: 92.81 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 218 SMQRQSSFIPGMH-IRLLDHQVQGLTWLKSretvSKSSASGGILADDMGLGKTIQMIALIlsHPLPKKKHSIKSTLVVAP 296
Cdd:cd18053 5 ALKKQPSYIGGHEgLELRDYQLNGLNWLAH----SWCKGNSCILADEMGLGKTIQTISFL--NYLFHEHQLYGPFLLVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 297 LSLIKQWESEVQT-KSKLTAIVYHGASRYKLLKVIHEY----------DVVITTYQILVsewvshnttgtdgkspteaks 365
Cdd:cd18053 79 LSTLTSWQREIQTwAPQMNAVVYLGDINSRNMIRTHEWmhpqtkrlkfNILLTTYEILL--------------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111970 366 yeKKKPSLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFndqSVWKD 443
Cdd:cd18053 138 --KDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF---SSWED 210
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
236-472 |
2.81e-20 |
|
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: 90.46 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWLKsretVSKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KSKLT 314
Cdd:cd18055 4 YQLEGLNWLR----FSWAQGTDTILADEMGLGKTIQTIVFLYS--LYKEGHTKGPFLVSAPLSTIINWEREFQMwAPDFY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 315 AIVYHGASRYKllKVIHEydvvittyqilvSEWVSHNTTGTDGKSPTEAK------------SYEK---KKPSLFAFYWW 379
Cdd:cd18055 78 VVTYTGDKDSR--AIIRE------------NEFSFDDNAVKGGKKAFKMKreaqvkfhvlltSYELvtiDQAALGSIRWA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 380 RIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISlpLCQGEENLvfK 459
Cdd:cd18055 144 CLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--DISKEDQI--K 219
|
250
....*....|...
gi 19111970 460 RLRMLLSVIMLRR 472
Cdd:cd18055 220 KLHDLLGPHMLRR 232
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
236-472 |
3.71e-20 |
|
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: 90.12 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWLKsretVSKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KSKLT 314
Cdd:cd18057 4 YQLEGLNWLR----FSWAQGTDTILADEMGLGKTVQTIVFLYS--LYKEGHSKGPYLVSAPLSTIINWEREFEMwAPDFY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 315 AIVYHGASRYKllKVIHEYDVVITTYQILVSEWVSHNTTGTDGKSPTEAKSYEK---KKPSLFAFYWWRIILDEAHTIKN 391
Cdd:cd18057 78 VVTYTGDKESR--SVIRENEFSFEDNAIRSGKKVFRMKKEAQIKFHVLLTSYELitiDQAILGSIEWACLVVDEAHRLKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 392 KSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISlPLCQGEEnlvFKRLRMLLSVIMLR 471
Cdd:cd18057 156 NQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-DISKEDQ---IKKLHDLLGPHMLR 231
|
.
gi 19111970 472 R 472
Cdd:cd18057 232 R 232
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
684-767 |
4.59e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 84.96 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 684 DIIDLHLRKAGIGFVRYDGRMNNRAREKSLDLLRSDSgTQVLLCSlKCGALGLNLTCASRVILCDVWWNPAIEEQAIDRV 763
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK-IKVLVAT-DVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 19111970 764 HRIG 767
Cdd:smart00490 79 GRAG 82
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
217-474 |
1.49e-19 |
|
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: 88.97 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 217 DSMQRQSSFIpgMHIRLLDHQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAP 296
Cdd:cd18063 10 ERVEKQSSLL--INGTLKHYQLQGLEWMVSL----YNNNLNGILADEMGLGKTIQTIALITY--LMEHKRLNGPYLIIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 297 LSLIKQWESEVQT-KSKLTAIVYHG--ASRYKLLKVIH--EYDVVITTYQILVsewvshnttgtdgkspteaksyeKKKP 371
Cdd:cd18063 82 LSTLSNWTYEFDKwAPSVVKISYKGtpAMRRSLVPQLRsgKFNVLLTTYEYII-----------------------KDKH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 372 SLFAFYWWRIILDEAHTIKNKSSK-SALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLP-- 448
Cdd:cd18063 139 ILAKIRWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfa 218
|
250 260 270
....*....|....*....|....*....|...
gi 19111970 449 -------LCQGEENLVFKRLRMLLSVIMLRRTK 474
Cdd:cd18063 219 mtgervdLNEEETILIIRRLHKVLRPFLLRRLK 251
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
217-474 |
1.74e-19 |
|
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: 88.95 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 217 DSMQRQSSFIpgMHIRLLDHQVQGLTWLKSRetvsKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAP 296
Cdd:cd18062 10 EKVEKQSSLL--VNGVLKQYQIKGLEWLVSL----YNNNLNGILADEMGLGKTIQTIALITY--LMEHKRINGPFLIIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 297 LSLIKQWESEVQT-KSKLTAIVYHG--ASRYKLLKVIH--EYDVVITTYQILVsewvshnttgtdgkspteaksyeKKKP 371
Cdd:cd18062 82 LSTLSNWVYEFDKwAPSVVKVSYKGspAARRAFVPQLRsgKFNVLLTTYEYII-----------------------KDKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 372 SLFAFYWWRIILDEAHTIKNKSSK-SALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLP-- 448
Cdd:cd18062 139 ILAKIRWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfa 218
|
250 260 270
....*....|....*....|....*....|...
gi 19111970 449 -------LCQGEENLVFKRLRMLLSVIMLRRTK 474
Cdd:cd18062 219 mtgekvdLNEEETILIIRRLHKVLRPFLLRRLK 251
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
236-433 |
1.77e-19 |
|
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350826 [Multi-domain] Cd Length: 246 Bit Score: 88.79 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWL-----KSRETVSKSSASGGILADDMGLGKTIQMIALILSHPLPKKKHSIKSTLVVAPLSLIKQWESEVQT- 309
Cdd:cd18068 4 HQVDGVQFMwdcccESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 310 ----KSKLTAIVYHGAS-------RYKLLKVIHEYDVVITTYqilvsEWVSHNTTGTDGKSPTEAKSYEKKK-----PSL 373
Cdd:cd18068 84 qeglKDEEKIEVNELATykrpqerSYKLQRWQEEGGVMIIGY-----DMYRILAQERNVKSREKLKEIFNKAlvdpgPDF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 374 fafywwrIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHIN 433
Cdd:cd18068 159 -------VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPN 211
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
233-472 |
2.55e-19 |
|
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: 87.98 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWL-KSRETVSKSSASGGILADDMGLGKTIQMIALI---LSHPLPKKKHSIKSTLVVAPLSLIKQWESEVQ 308
Cdd:cd18066 1 LRPHQREGIEFLyECVMGMRVNERFGAILADEMGLGKTLQCISLIwtlLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 309 TkskltaivYHGASRYKLLKVIHE-----------YDVVITTYQILVsewvshnttgtdgkspteaKSYEKKKPSLFAFy 377
Cdd:cd18066 81 K--------WLGSERIKVFTVDQDhkveefiasplYSVLIISYEMLL-------------------RSLDQISKLNFDL- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 378 wwrIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQG----- 452
Cdd:cd18066 133 ---VICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSrepta 209
|
250 260
....*....|....*....|....*.
gi 19111970 453 ---EENLVFKR---LRMLLSVIMLRR 472
Cdd:cd18066 210 tpeEKKLGEARaaeLTRLTGLFILRR 235
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
236-454 |
6.55e-19 |
|
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: 86.76 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWL-KSRETVSKSSASGGILADDMGLGKTIQMIALI--LSHPLPKKKHSIKSTLVVAPLSLIKQWESEVqTK-- 310
Cdd:cd18067 4 HQREGVKFLyRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMwtLLRQSPQCKPEIDKAIVVSPSSLVKNWANEL-GKwl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 311 -SKLTAIVYHGASRykllkviheydvvittYQILVSEWVSHNTTGTDGKSPTEAKSYEKKKPSLFAFYWWRI---ILDEA 386
Cdd:cd18067 83 gGRLQPLAIDGGSK----------------KEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVglvICDEG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111970 387 HTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQGEE 454
Cdd:cd18067 147 HRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRD 214
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
259-472 |
3.04e-18 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350769 [Multi-domain] Cd Length: 207 Bit Score: 83.88 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 259 ILADDMGLGKTIQMIALILSHplpKKKHSIKSTLVVAPLSLIKQWESEVQTKSKLTAIVYHGASRYKLLKVI----HEYD 334
Cdd:cd18011 21 LLADEVGLGKTIEAGLIIKEL---LLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLIgnpfEEFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 335 VVITTYQILVSewvshnttgtdgkspteaksyEKKKPSLFAFYWWR-IILDEAHTIKN----KSSKSALACCALQGINRW 409
Cdd:cd18011 98 IVIVSLDLLKR---------------------SEERRGLLLSEEWDlVVVDEAHKLRNsgggKETKRYKLGRLLAKRARH 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111970 410 C--LTGTPLQNNVDELYSLVKFLHINPFNDQsvwkdqislplcqgEENLVFKRLRMLLSVIMLRR 472
Cdd:cd18011 157 VllLTATPHNGKEEDFRALLSLLDPGRFAVL--------------GRFLRLDGLREVLAKVLLRR 207
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
236-472 |
3.67e-18 |
|
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: 84.35 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWLKsretVSKSSASGGILADDMGLGKTIQMIALILShpLPKKKHSIKSTLVVAPLSLIKQWESEVQT-KSKLT 314
Cdd:cd18056 4 YQLEGLNWLR----FSWAQGTDTILADEMGLGKTVQTAVFLYS--LYKEGHSKGPFLVSAPLSTIINWEREFEMwAPDMY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 315 AIVYHGASRYKllKVIHEYDVVITTYQILVSEWVSHNTTGTDGKSPTEAKSYEK---KKPSLFAFYWWRIILDEAHTIKN 391
Cdd:cd18056 78 VVTYVGDKDSR--AIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELitiDMAILGSIDWACLIVDEAHRLKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 392 KSSK--SALACCALQgiNRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISlPLCQGEEnlvFKRLRMLLSVIM 469
Cdd:cd18056 156 NQSKffRVLNGYSLQ--HKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA-DIAKEDQ---IKKLHDMLGPHM 229
|
...
gi 19111970 470 LRR 472
Cdd:cd18056 230 LRR 232
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
236-430 |
1.67e-17 |
|
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350827 [Multi-domain] Cd Length: 227 Bit Score: 82.56 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 236 HQVQGLTWL-----KSRETVSKSSASGGILADDMGLGKTIQMIALI---LSHPlpkkkhSIKSTLVVAPLSLIKQWESEV 307
Cdd:cd18069 4 HQIGGIRFLydniiESLERYKGSSGFGCILAHSMGLGKTLQVISFLdvlLRHT------GAKTVLAIVPVNTLQNWLSEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 308 QTksKLTAIVYHGASRYKLLKVIHEYDVVITTYQI--LVSEWVSHNTTGTDGkspteaksYE----KKKPSLfafywwrI 381
Cdd:cd18069 78 NK--WLPPPEALPNVRPRPFKVFILNDEHKTTAARakVIEDWVKDGGVLLMG--------YEmfrlRPGPDV-------V 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19111970 382 ILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFL 430
Cdd:cd18069 141 ICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFV 189
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
233-430 |
1.22e-15 |
|
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: 76.47 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLTWLKSREtvskssasGGIL-ADDMGLGKTIQMIAlILSH-----PLpkkkhsikstLVVAPLSLIKQWESE 306
Cdd:cd18010 1 LLPFQREGVCFALRRG--------GRVLiADEMGLGKTVQAIA-IAAYyreewPL----------LIVCPSSLRLTWADE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 307 VQtkskltaivyhgasRYkLLKVIHEYDVVIttyqilvsewvshnTTGTDGKSPTEAK----SYE---KKKPSLFAFYWW 379
Cdd:cd18010 62 IE--------------RW-LPSLPPDDIQVI--------------VKSKDGLRDGDAKvvivSYDllrRLEKQLLARKFK 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19111970 380 RIILDEAHTIKNKSSKSALACCAL-QGINR-WCLTGTPLQNNVDELYSLVKFL 430
Cdd:cd18010 113 VVICDESHYLKNSKAKRTKAALPLlKRAKRvILLSGTPALSRPIELFTQLDAL 165
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
235-430 |
1.31e-09 |
|
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: 58.90 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 235 DHQVQGLTWLKSRETvskssasGGILADdMGLGKTIQMIALILSHPLPKKKHSIkstLVVAPLSLIKQ-WESEVQ----- 308
Cdd:cd18013 3 PYQKVAINFIIEHPY-------CGLFLD-MGLGKTVTTLTALSDLQLDDFTRRV---LVIAPLRVARStWPDEVEkwnhl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 309 TKSKLTAIVYHGASRYKLLKVihEYDVVITTYQILvsEWVshnttgtdgkspteAKSYEKKKPslfafyWWRIILDEAHT 388
Cdd:cd18013 72 RNLTVSVAVGTERQRSKAANT--PADLYVINRENL--KWL--------------VNKSGDPWP------FDMVVIDELSS 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19111970 389 IKNKSSKSALACCALQG-INRWC-LTGTPLQNNVDELYSLVKFL 430
Cdd:cd18013 128 FKSPRSKRFKALRKVRPvIKRLIgLTGTPSPNGLMDLWAQIALL 171
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
227-415 |
3.88e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 56.96 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 227 PGMHIRLLDHQVQGL-TWLKSRETVSKSsasgGILADDMGLGKTIQMIALIlshplpKKKHSIKSTLVVAP-LSLIKQWE 304
Cdd:COG1061 75 SGTSFELRPYQQEALeALLAALERGGGR----GLVVAPTGTGKTVLALALA------AELLRGKRVLVLVPrRELLEQWA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 305 SEVqtKSKLTAIVYHGASRYKllkvihEYDVVITTYQILVSewvshnttgtdgkspteaksyeKKKPSLFAFYWWRIILD 384
Cdd:COG1061 145 EEL--RRFLGDPLAGGGKKDS------DAPITVATYQSLAR----------------------RAHLDELGDRFGLVIID 194
|
170 180 190
....*....|....*....|....*....|.
gi 19111970 385 EAHTIKNKSSKSALAccALQGINRWCLTGTP 415
Cdd:COG1061 195 EAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
233-415 |
7.64e-08 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 52.31 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 233 LLDHQVQGLT-WLKSRetvsksSASGGILADDMGLGKTIQMIALILshplpkkKHSIKSTLVVAP-LSLIKQWESEVQTK 310
Cdd:cd17926 1 LRPYQEEALEaWLAHK------NNRRGILVLPTGSGKTLTALALIA-------YLKELRTLIVVPtDALLDQWKERFEDF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 311 SKLTAIVYHGASRYKLLKVIheyDVVITTYQILVSEwvshnttgtdgkspteaksyEKKKPSLFAFYWWrIILDEAHTIK 390
Cdd:cd17926 68 LGDSSIGLIGGGKKKDFDDA---NVVVATYQSLSNL--------------------AEEEKDLFDQFGL-LIVDEAHHLP 123
|
170 180
....*....|....*....|....*
gi 19111970 391 NKSSKSALAccALQGINRWCLTGTP 415
Cdd:cd17926 124 AKTFSEILK--ELNAKYRLGLTATP 146
|
|
| PRK04914 |
PRK04914 |
RNA polymerase-associated protein RapA; |
719-786 |
1.16e-05 |
|
RNA polymerase-associated protein RapA;
Pssm-ID: 235319 [Multi-domain] Cd Length: 956 Bit Score: 49.07 E-value: 1.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111970 719 DSGTQVLLCSlKCGALGLNLTCASRVILCDVWWNPAIEEQAIDRVHRIGQRRDVLVYKLVVENTIEEK 786
Cdd:PRK04914 544 EDGAQVLLCS-EIGSEGRNFQFASHLVLFDLPFNPDLLEQRIGRLDRIGQKHDIQIHVPYLEGTAQER 610
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
255-387 |
3.23e-05 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 44.70 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 255 ASGGILADDMGLGKTIQ-MIALILSHPLPKKKhsiksTLVVAPL-SLIKQWESEVQT--KSKLTAIVYHGASRYKLL--K 328
Cdd:cd00046 1 GENVLITAPTGSGKTLAaLLAALLLLLKKGKK-----VLVLVPTkALALQTAERLRElfGPGIRVAVLVGGSSAEERekN 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 19111970 329 VIHEYDVVITTYQILVSewvshnttgtdgKSPTEAKSYEKKkpslfafyWWRIILDEAH 387
Cdd:cd00046 76 KLGDADIIIATPDMLLN------------LLLREDRLFLKD--------LKLIIVDEAH 114
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
265-389 |
1.22e-04 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 43.39 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 265 GLGKT-IQMIALI--LSHPLPKKKhsiksTLVVAPL-SLIKQWESEVQTKSKLTAI----VYHGASRYKLLKVIHEYDVV 336
Cdd:pfam00270 24 GSGKTlAFLLPALeaLDKLDNGPQ-----ALVLAPTrELAEQIYEELKKLGKGLGLkvasLLGGDSRKEQLEKLKGPDIL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 19111970 337 ITTYQILVSEWVSHNTTgtdgkspteaksyekKKPSLfafywwrIILDEAHTI 389
Cdd:pfam00270 99 VGTPGRLLDLLQERKLL---------------KNLKL-------LVLDEAHRL 129
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
709-775 |
7.43e-04 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 38.84 E-value: 7.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111970 709 REKSLDLLRSdsgTQVLLCSLKCGaLGLNLTCASRVILCDVWWNPAIEEQAIDRVHRIGQRRDVLVY 775
Cdd:cd18785 13 IEHAEEIASS---LEILVATNVLG-EGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
634-781 |
1.20e-03 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 42.32 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 634 GIQDPNDKTLYKSSKIREIL-KILSLDEQEEDDTVR-------GLRKTIIFSQFTTFLDIIDLHLRKAGIGFVRYDGRMN 705
Cdd:COG1061 261 GIRVDLTDERAEYDALSERLrEALAADAERKDKILRellrehpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTP 340
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111970 706 NRAREKSLDLLRsdSGTQVLLCSLKCGALGLNLTCASRVILCDVWWNPAIEEQAIDRVHRIGQR-RDVLVYKLVVEN 781
Cdd:COG1061 341 KKEREEILEAFR--DGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGkEDALVYDFVGND 415
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
265-387 |
5.48e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 38.31 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111970 265 GLGKTiqMIALILSHPLpKKKHSIKSTLVVAP-LSLIKQWESEVQT-KSKLTAIVYHGASrykllKVIHEYDVVITTYQI 342
Cdd:cd18032 30 GTGKT--YTAAFLIKRL-LEANRKKRILFLAHrEELLEQAERSFKEvLPDGSFGNLKGGK-----KKPDDARVVFATVQT 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 19111970 343 LVSEwvshnttgtdgkspteaKSYEKKKPSLFAFywwrIILDEAH 387
Cdd:cd18032 102 LNKR-----------------KRLEKFPPDYFDL----IIIDEAH 125
|
|
| |
