|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04914 |
PRK04914 |
RNA polymerase-associated protein RapA; |
2-966 |
0e+00 |
|
RNA polymerase-associated protein RapA;
Pssm-ID: 235319 [Multi-domain] Cd Length: 956 Bit Score: 1890.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 2 PFTLGQRWISDTESELGLGTVVAIDTRMVTLLFPATGENRLYARNDSPVTRVMFNPGDTVTSHDGWQLKIEDVKEENGLL 81
Cdd:PRK04914 1 PFALGQRWISDTESELGLGTVVAVDGRTVTLLFPATGENRLYARNDAPLTRVMFNPGDTITSHEGWQLTVEEVEEENGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 82 AYIGTRLDTDEANVVLREVLLDSKLVFSKPQDRLFAGQIDRMDRFSLRYRARKFQSEQYRMPWSGLRGQRTSLIPHQLNI 161
Cdd:PRK04914 81 TYHGTRLDTEEEGVALRETFLDSKIRFNKPQDRLFAGQIDRMDRFALRYRALKHQSEQFQSPLRGLRGARASLIPHQLYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 162 AHDVGRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMLRRFNLRFSLFDDERYAEAQHD 241
Cdd:PRK04914 161 AHEVGRRHAPRVLLADEVGLGKTIEAGMIIHQQLLTGRAERVLILVPETLQHQWLVEMLRRFNLRFSLFDEERYAEAQHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 242 ADNPFETEQLVICSLDFVRRSKQRLEHLCDAEWDIMVVDEAHHLVWSEDAPSREYMAIEQLAERVPGVLLLTATPEQLGL 321
Cdd:PRK04914 241 ADNPFETEQLVICSLDFLRRNKQRLEQALAAEWDLLVVDEAHHLVWSEEAPSREYQVVEQLAEVIPGVLLLTATPEQLGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 322 ESHFARLRLLDPNRFHDFAQFVEEQNNYRPVADAVAMLLAGKRLSDDELNTLSDLIGEQDIEPLLQAANSDSDNAESARK 401
Cdd:PRK04914 321 ESHFARLRLLDPDRFHDYEAFVEEQQQYRPVADAVQALLAGEKLSDDALNALGELLGEQDIEPLLQAANSDSEEAQAARQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 402 ELIDMLMDRHGTSRVLFRNTRNGVKGFPKRELHTIKLPLPTQYQTAIKVsgimgarkTQEERARDMLYPEQIYQEFEgDT 481
Cdd:PRK04914 401 ELISELLDRHGTGRVLFRNTRAAVKGFPKRELHPIPLPLPEQYQTAIKV--------SLEARARDMLYPEQIYQEFE-DN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 482 GTWWNFDPRVEWLMGYLTAHRSRKVLVICAKAATALQLEQVLREREGIRAAVFHEGMSIVERDRAAAWFGEEDSGAQVLL 561
Cdd:PRK04914 472 ATWWNFDPRVEWLIDFLKSHRSEKVLVICAKAATALQLEQALREREGIRAAVFHEGMSIIERDRAAAYFADEEDGAQVLL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 562 CSEIGSEGRNFQFASNLVMFDLPFNPDLLEQRIGRLDRIGQAHDIQIHVPYLEKTAQSVLVRWFHEGLDAFEHTCPTGRT 641
Cdd:PRK04914 552 CSEIGSEGRNFQFASHLVLFDLPFNPDLLEQRIGRLDRIGQKHDIQIHVPYLEGTAQERLFRWYHEGLNAFEHTCPTGRA 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 642 IYDQVHGDLIGYLAAPENAEGFDELIKSCREKHDALKAQLEQGRDRLLEIHSNGGEKAQALAESIEEQDDDTSLISFSMN 721
Cdd:PRK04914 632 LYDEFGDELIPYLASPDDTDGLDELIAETREQHEALKAQLEQGRDRLLELNSCGGEKAQALAEAIAEQDDDTNLVNFALN 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 722 LFDIVGINQDDRGENLIVLTPSDHMLVPDFPGLPEDGCTITFERDVALSREDAQFITWEHPLIRNGLDLILSGDTGSSTI 801
Cdd:PRK04914 712 LFDIIGINQEDRGENAIVLTPSDHMLVPDFPGLPEDGVTITFDRDQALSREDMQFLTWEHPLIRGGLDLILSGDTGSTAV 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 802 SLLKNKALPVGTLLLELIYVVEAQAPKQLQLTRFLPPTPVRLLLDKNGTNLAGQVEFESFNRQLSAVNRHTGSKLVNAVQ 881
Cdd:PRK04914 792 ALLKNKALPAGTLLLELIYVVEAQAPKSLQLTRFLPPTPVRLLLDKNGNDLSAQVEFESLNRQLSAVNRHTASKLVKAVQ 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 882 QDVHAILQLGETQIEKAARALIDAARSEADEKLSAELSRLEALKAVNPNIRDDELAAIESNRQQVLESLNQAGWRLDALR 961
Cdd:PRK04914 872 QDIHKLLQKAEAQAEAQARELIEQAKQEADEKLSAELSRLEALKAVNPNIRDDEIEALESQRQEVLEALDQAQLRLDAIR 951
|
....*
gi 556425441 962 LIVVT 966
Cdd:PRK04914 952 LIVVT 956
|
|
| RapA_C |
pfam12137 |
RNA polymerase recycling family C-terminal; This domain is found in bacteria. This domain is ... |
605-964 |
0e+00 |
|
RNA polymerase recycling family C-terminal; This domain is found in bacteria. This domain is about 360 amino acids in length. This domain is found associated with pfam00271, pfam00176. The function of this domain is not known, but structurally it forms an alpha-beta fold in nature with a central beta-sheet flanked by helices and loops, the beta-sheet being mainly antiparallel and flanked by four alpha helices, among which the two longer helices exhibit a coiled-coil arrangement.
Pssm-ID: 432354 Cd Length: 359 Bit Score: 584.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 605 DIQIHVPYLEKTAQSVLVRWFHEGLDAFEHTCPTGRTIYDQVHGDLIGYLAAPEnAEGFDELIKSCREKHDALKAQLEQG 684
Cdd:pfam12137 1 DIQIHVPYLEGSAQEVLFRWYHEGLNAFEQTCPAGQAVYEEFGDRLLDLLAAPD-EEALEALIAETRALREALKAELEQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 685 RDRLLEIHSNGGEKAQALAESIEEQDDDTSLISFSMNLFDIVGINQDDRGENLIVLTPSDHMLVPDFPGLPEDGCTITFE 764
Cdd:pfam12137 80 RDRLLELNSCRPERAEALVEAIAEEDDDTELADFMERLFDAFGVDQEDHSEGSIVLRPSDHMLVPDFPGLPEDGMTVTFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 765 RDVALSREDAQFITWEHPLIRNGLDLILSGDTGSSTISLLKNKALPVGTLLLELIYVVEAQAPKQLQLTRFLPPTPVRLL 844
Cdd:pfam12137 160 RDTALAREDLQFLTWEHPMVRGAMDLILSSDTGNAAVALLKNKALPAGTLLLELIFVVECVAPKALQLDRFLPPTPIRLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 845 LDKNGTNLAGQVEFESFNRQLSAVNRHTGSKLVNAVQQDVHAILQLGETQIEKAARALIDAARSEADEKLSAELSRLEAL 924
Cdd:pfam12137 240 LDKKGNDLSAKVPFESLNRQLSPVNRHTARKLVKAQRDLIEKLLAKAEQLAEEQAEALIEQAKARMDQTLSAELERLEAL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 556425441 925 KAVNPNIRDDELAAIESNRQQVLESLNQAGWRLDALRLIV 964
Cdd:pfam12137 320 QAVNPNIRDDEIEALEEQRAQLLAALDQARLRLDAIRLIV 359
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
1-636 |
7.99e-109 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 352.22 E-value: 7.99e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 1 MPFTLGQRWISDTESELGLGTVVAIDTRMVTLLFPATGENRLYARNDSPVTRVMFNPGDTVTSHDGWQLKIEDVKEENGL 80
Cdd:COG0553 109 LLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 81 LAYIGTRLDTDEAnVVLREVLLDSKLVFSKPQDRLfagqidrmdrfslryRARKFQSEQYRMPwSGLRGQrtsLIPHQLN 160
Cdd:COG0553 189 LLELALLAAEAEL-LLLLELLLELELLAEAAVDAF---------------RLRRLREALESLP-AGLKAT---LRPYQLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 161 IAHDVG--RRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMlRRFN--LRFSLFDDERya 236
Cdd:COG0553 249 GAAWLLflRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQREL-AKFApgLRVLVLDGTR-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 237 eAQHDADNPFETEQLVICSLDFVRRSkqrLEHLCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLaeRVPGVLLLTATP 316
Cdd:COG0553 326 -ERAKGANPFEDADLVITSYGLLRRD---IELLAAVDWDLVILDEAQHI---KNPATKRAKAVRAL--KARHRLALTGTP 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 317 EQLGLESHFARLRLLDPNRFHDFAQFVEEQNNYRPVADAVAMllagkrlsdDELNTLsdligeqdiepllqaansdsdna 396
Cdd:COG0553 397 VENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEAL---------ERLRRL----------------------- 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 397 esarkelidmlmdrhgTSRVLFRNTRNGV-KGFPKRELHTIKLPL-PTQ---YQTAIK-VSGIMGARKTQEERAR--DML 468
Cdd:COG0553 445 ----------------LRPFLLRRTKEDVlKDLPEKTEETLYVELtPEQralYEAVLEyLRRELEGAEGIRRRGLilAAL 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 469 --------YPEQIYQEFEGDTGTwwnfDPRVEWLMGYLTAHRS--RKVLVICAKAATALQLEQVLREReGIRAAVFHEGM 538
Cdd:COG0553 509 trlrqicsHPALLLEEGAELSGR----SAKLEALLELLEELLAegEKVLVFSQFTDTLDLLEERLEER-GIEYAYLHGGT 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 539 SIVERDRAAAWFGEEDSGAQVLLCSEIGSEGRNFQFASNLVMFDLPFNPDLLEQRIGRLDRIGQAHDIQIHVPYLEKTAQ 618
Cdd:COG0553 584 SAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIE 663
|
650
....*....|....*...
gi 556425441 619 SVLVRWFHEGLDAFEHTC 636
Cdd:COG0553 664 EKILELLEEKRALAESVL 681
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
154-345 |
4.28e-70 |
|
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: 231.41 E-value: 4.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 154 LIPHQLNIAHDVGRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMLRRFNLRFSLFDDE 233
Cdd:cd18011 1 PLPHQIDAVLRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 234 RYAEAQHDADNPFETEQLVICSLDFVRRSKQRLEHLCDAEWDIMVVDEAHHLVWSEDA-PSREYMAIEQLAERVPGVLLL 312
Cdd:cd18011 81 TAAQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSGGGkETKRYKLGRLLAKRARHVLLL 160
|
170 180 190
....*....|....*....|....*....|...
gi 556425441 313 TATPEQLGLESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd18011 161 TATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL 193
|
|
| DpdE |
NF041062 |
protein DpdE; |
154-966 |
1.49e-62 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 230.63 E-value: 1.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 154 LIPHQLNIAHDVGRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMLRRFNLrfslfDDe 233
Cdd:NF041062 154 LEPHQVAVVRRVLQDPVQRYLLADEVGLGKTIEAGLVIRQHLLDNPDARVLVLVPDALVRQWRRELRDKFFL-----DD- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 234 ryaeaqhdadnpFETEQLVICSLDFVRRSKQRLEHLcdaewDIMVVDEAHHLV---WSEDAPSRE-YMAIEQLAERVPGV 309
Cdd:NF041062 228 ------------FPGARVRVLSHEEPERWEPLLDAP-----DLLVVDEAHQLArlaWSGDPPERArYRELAALAHAAPRL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 310 LLLTATPEQLGLESHFARLRLLDPNRF-----HDFAQFVEEQNNYRPV-----ADAVAMLLagkrlsDDELNTLSDLIGE 379
Cdd:NF041062 291 LLLSATPVLGNEETFLALLHLLDPDLYplddlEAFRERLEEREELGRLvlgldPDNPNFLL------RQALDELRALFPE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 380 QD-----IEPLLQAANSDSDNAESARKELIDMLM----DRHGTSRVLFRNTRNGVKG----FPKRE-LHTIKLPLPT--- 442
Cdd:NF041062 365 DEelqelAEELLPLLDEFDDEEPEERARAVSALRahisETYRLHRRMIRNRRSSVLGadylVPGRAgPRVLVWESPArea 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 443 ------QYQTAIKVSGimgarkTQEERARDMLYpEQIYQEFEGDTGTWWNFDPRVEWLMGYLTAH--------------- 501
Cdd:NF041062 445 adealeDWREEAALLD------AESDPAARAAY-ARALAWLVARLGGPDDLAALLRWRLRGDAASadlagerellealia 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 502 ------------------------RSRKVLVICAKAATALQLEQVLREREGIRAAVFHEGMSIVERDRAAAWFgEEDSGA 557
Cdd:NF041062 518 aledeakdadllaaladwllpllrGSGKAVVFCGDGSLADHLAAALARLGAGSVERHLSGQGADQAERAVRAF-RQDPSA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 558 QVLLCSEIGSEGRNFQFASNLVMFDLPFNPDLLEQRIGRLDRIGQAHDIQI--HVPYLEKTAQSVLVRWF---HEGLDAF 632
Cdd:NF041062 597 RVLVCDRSGEEGLNLQGADRLVHLDLPWSPNRLEQRIGRLDRYASLRGGRPveSYVLAPSDDDSLYSAWAdllREGFGVF 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 633 EHTCPTGRTIYDQVHGDLIGyLAAPENAEGFDELIkscrekhDALKAQLEQGR------DRLLEIHsNGGEKAQALAESI 706
Cdd:NF041062 677 DRSVASLQDALDEGLDEAWR-ALLEEGPEALLEAI-------ARLRGELARERrrideqDALDSIE-ADAEEARSFAEAL 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 707 EEQDDDTSLISFSMN-------LFDIVGiNQDDRGENLIVLTP----SDHMLVPDFpgLPEDGCTITFERDVALSREDAQ 775
Cdd:NF041062 748 AEAEEDADELRDALLgwitkglRFRKRR-DEVDDVFRFDFASRrtllPPRLLIRRF--LPGLDREGTFSRSVALRRPGVR 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 776 FITWEHPLIRNGLDLILSGDTGSST--ISLLKNKALPvGTLLLELIYVVEAQAPKQLQLT-------------RFLPPTP 840
Cdd:NF041062 825 LFRYGNPFVDALARLLRWDDRGQAFamWRLDPSWRGE-PRLYFRFDFLVEADLLPALALLdgaarralrrradRLFPPFT 903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 841 VRLLLDKNGTnlagQVEFESFNRQLSAVNRHTGSK------LVNAVQQDVHAILQLGE-----TQIEKAARAL------- 902
Cdd:NF041062 904 LRVWVDADGE----EVTDPELLAWLNAPYSKPGGVggrdynLNGSRWEALLELFGADEwrelcRAAEEAARALlrsradl 979
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556425441 903 ---IDAARSEADEKLSAELSRLEALKAVNPNIRDDELAAIESNRQQVL-ESLNQAGWRLDALRLIVVT 966
Cdd:NF041062 980 aeaCARAQARARADLAVRLAQLRARAAAGSLVEDAEELAREVALAQALaDGIRNPSVRLDAVGCVVLS 1047
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
154-333 |
8.56e-39 |
|
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: 142.32 E-value: 8.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 154 LIPHQLNIAHDVGRR--HAPRVLLADEVGLGKTIEAGMILHQQLLSGA-AERVLIVVPETLQHQWLVEMLRRF-NLRFSL 229
Cdd:cd17919 1 LRPYQLEGLNFLLELyeNGPGGILADEMGLGKTLQAIAFLAYLLKEGKeRGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 230 FDDERYAEAQHDADNPFETEQLVICSLDFVRRSKqrlEHLCDAEWDIMVVDEAHHLVWSEdapSREYMAIEQLaeRVPGV 309
Cdd:cd17919 81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDK---ASLRKFRWDLVVVDEAHRLKNPK---SQLSKALKAL--RAKRR 152
|
170 180
....*....|....*....|....
gi 556425441 310 LLLTATPEQLGLESHFARLRLLDP 333
Cdd:cd17919 153 LLLTGTPLQNNLEELWALLDFLDP 176
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
170-315 |
5.64e-29 |
|
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: 112.88 E-value: 5.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 170 APRVLLADEVGLGKTIEAGMILHQQLLSgAAERVLIVVPE-TLQHQWLVEMLRRF--NLRFSLFDDERYAEAQHDADNPf 246
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK-KGKKVLVLVPTkALALQTAERLRELFgpGIRVAVLVGGSSAEEREKNKLG- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556425441 247 eTEQLVICSLDFVRRSKQRLEHLCDAEWDIMVVDEAHHLVWSEDAPSREYMAIEQLAERVPGVLLLTAT 315
Cdd:cd00046 79 -DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
488-609 |
2.00e-28 |
|
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: 111.03 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 488 DPRVEWLMGYLTAHRS--RKVLVICAKAATALQLEQVLREReGIRAAVFHEGMSIVERDRAAAWFGEEDSGAQVLLCSEI 565
Cdd:cd18793 10 SGKLEALLELLEELREpgEKVLIFSQFTDTLDILEEALRER-GIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 556425441 566 GSEGRNFQFASNLVMFDLPFNPDLLEQRIGRLDRIGQAHDIQIH 609
Cdd:cd18793 89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVY 132
|
|
| Tudor_RapA |
pfam18337 |
RapA N-terminal Tudor like domain; This is one of two Tudor-like domains found in the ... |
55-118 |
3.06e-27 |
|
RapA N-terminal Tudor like domain; This is one of two Tudor-like domains found in the N-terminal region of RapA proteins. RapA is an abundant RNAP-associated protein of 110-kDa molecular weight with ATPase activity. It forms a stable complex with the RNAP core enzyme, but not with the holoenzyme. The ATPase activity of RapA increases upon its binding to RNAP. The N-terminal region of RapA contains two copies of a Tudor-like domains, both folded as a highly bent antiparallel beta-sheet. This fold is also found in transcription factor NusG, ribosomal protein L24, human SMN (survival of motor neuron) protein, mammalian DNA repair factor 53BP1, putative fission yeast DNA repair factor Crb2 and bacterial transcription-repair coupling factor known as Mfd. The functional roles of the N-terminal region homologs in these proteins suggest that the Tudor-like domains of RapA may interact with both nucleic acids and RNAP.
Pssm-ID: 465716 [Multi-domain] Cd Length: 62 Bit Score: 104.89 E-value: 3.06e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425441 55 FNPGDTVTSHDGWQLKIEDVKEENGLLAYIGTRLDTDEanVVLREVLLDSKLVFSKPQDRLFAG 118
Cdd:pfam18337 1 FNVGDTITSHEGWKLTVEEVEEENGLLIYLGTREDGEE--VSLPETELDHFIQFNKPQDRLFAG 62
|
|
| Tudor_1_RapA |
pfam18339 |
RapA N-terminal Tudor like domain 1; This is one of two Tudor-like domains found in the ... |
3-53 |
4.09e-27 |
|
RapA N-terminal Tudor like domain 1; This is one of two Tudor-like domains found in the N-terminal region of RapA proteins. RapA is an abundant RNAP-associated protein of 110-kDa molecular weight with ATPase activity. It forms a stable complex with the RNAP core enzyme, but not with the holoenzyme. The ATPase activity of RapA increases upon its binding to RNAP. The N-terminal region of RapA contains two copies of a Tudor-like domains, both folded as a highly bent antiparallel beta-sheet. This fold is also found in transcription factor NusG, ribosomal protein L24, human SMN (survival of motor neuron) protein, mammalian DNA repair factor 53BP1, putative fission yeast DNA repair factor Crb2 and bacterial transcription-repair coupling factor known as Mfd. The functional roles of the N-terminal region homologs in these proteins suggest that the Tudor-like domains of RapA may interact with both nucleic acids and RNAP.
Pssm-ID: 436422 [Multi-domain] Cd Length: 51 Bit Score: 104.49 E-value: 4.09e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 556425441 3 FTLGQRWISDTESELGLGTVVAIDTRMVTLLFPATGENRLYARNDSPVTRV 53
Cdd:pfam18339 1 FAPGQRWISDTEPELGLGIVVEVDGRTVTILFPASGETRTYATANAPLTRV 51
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
490-601 |
8.10e-20 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 85.73 E-value: 8.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 490 RVEWLMGYLTAHRSRKVLVICAKAATALqlEQVLREREGIRAAVFHEGMSIVERDRAAAWFGEEDSgaQVLLCSEIGSEG 569
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKI--DVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 556425441 570 RNFQFASNLVMFDLPFNPDLLEQRIGRLDRIG 601
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
152-336 |
4.42e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 152 TSLIPHQLNIAHDVgRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVP-ETLQHQWLVEMLRRF----NLR 226
Cdd:smart00487 7 EPLRPYQKEAIEAL-LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGpslgLKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 227 FSLFDDERYAEAQHDADNpfETEQLVICSLDFVRRSKQRlEHLCDAEWDIMVVDEAHHLvwSEDAPSREYMAIEQLAERV 306
Cdd:smart00487 86 VGLYGGDSKREQLRKLES--GKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRL--LDGGFGDQLEKLLKLLPKN 160
|
170 180 190
....*....|....*....|....*....|
gi 556425441 307 PGVLLLTATPEQLGLEshFARLRLLDPNRF 336
Cdd:smart00487 161 VQLLLLSATPPEEIEN--LLELFLNDPVFI 188
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
518-601 |
5.82e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 70.70 E-value: 5.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 518 QLEQVLREReGIRAAVFHEGMSIVERDRAAAWFGEEDSgaQVLLCSEIGSEGRNFQFASNLVMFDLPFNPDLLEQRIGRL 597
Cdd:smart00490 2 ELAELLKEL-GIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 556425441 598 DRIG 601
Cdd:smart00490 79 GRAG 82
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
174-342 |
1.02e-14 |
|
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: 75.80 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEA----GMILHQQLLSGAAerVLIVVPETLQHQWLVEMLRRFNL----RFSLFDDERYAEAQHDADNP 245
Cdd:pfam00176 21 ILADEMGLGKTLQTisllLYLKHVDKNWGGP--TLIVVPLSLLHNWMNEFERWVSPpalrVVVLHGNKRPQERWKNDPNF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 246 FETEQLVICSLDFVRRSKqrlEHLCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLaeRVPGVLLLTATPEQLGLESHF 325
Cdd:pfam00176 99 LADFDVVITTYETLRKHK---ELLKKVHWHRIVLDEGHRL---KNSKSKLSKALKSL--KTRNRWILTGTPLQNNLEELW 170
|
170
....*....|....*..
gi 556425441 326 ARLRLLDPNRFHDFAQF 342
Cdd:pfam00176 171 ALLNFLRPGPFGSLSTF 187
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
166-342 |
5.26e-14 |
|
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: 72.70 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 166 GRRHAPR--VLLADEVGLGKTIEAGMILHQQLLSGA-----AERVLIVVPETLQHQWLVEMLRRFNLRF----SLFDDER 234
Cdd:cd18004 18 GRRGYGGggAILADEMGLGKTLQAIALVWTLLKQGPygkptAKKALIVCPSSLVGNWKAEFDKWLGLRRikvvTADGNAK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 235 YAEAQHDADNPFETEQLVICSLDFVRRSKQRLEhlCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLaeRVPGVLLLTA 314
Cdd:cd18004 98 DVKASLDFFSSASTYPVLIISYETLRRHAEKLS--KKISIDLLICDEGHRL---KNSESKTTKALNSL--PCRRRLLLTG 170
|
170 180
....*....|....*....|....*...
gi 556425441 315 TPEQLGLESHFARLRLLDPNRFHDFAQF 342
Cdd:cd18004 171 TPIQNDLDEFFALVDFVNPGILGSLASF 198
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
168-340 |
9.99e-14 |
|
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: 71.08 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 168 RHAPRVLLADEVGLGKTIEAGMILHqqllsgaAER----VLIVVPETLQHQWlVEMLRRFnLRFSLFDDERYAEAQHDAD 243
Cdd:cd18010 14 RRGGRVLIADEMGLGKTVQAIAIAA-------YYReewpLLIVCPSSLRLTW-ADEIERW-LPSLPPDDIQVIVKSKDGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 244 NPFETeQLVICSLDFVRRSKqrlEHLCDAEWDIMVVDEAHHLVWSEDAPSREYMAIEQLAERvpgVLLLTATP-----EQ 318
Cdd:cd18010 85 RDGDA-KVVIVSYDLLRRLE---KQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKR---VILLSGTPalsrpIE 157
|
170 180
....*....|....*....|....*
gi 556425441 319 LgleshFARLRLLDP---NRFHDFA 340
Cdd:cd18010 158 L-----FTQLDALDPklfGRFHDFG 177
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
83-712 |
3.23e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 70.44 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 83 YIGTRLDTDEANVVLREVLLDSKLVFSKPQDRLFAGQIDRMDRFSLRYRARKFQSEQYRMPWSGLRGQRTSLIPHQ---L 159
Cdd:COG1061 10 GADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQqeaL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 160 NIAHDVGRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGaaeRVLIVVP-ETLQHQWlVEMLRRFNLRFSLFDDERYAEA 238
Cdd:COG1061 90 EALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPrRELLEQW-AEELRRFLGDPLAGGGKKDSDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 239 QHdadnpfeteqlVICSLDFVRRsKQRLEHLCDAeWDIMVVDEAHHlvwsedAPSREYmaiEQLAERVPG--VLLLTATP 316
Cdd:COG1061 166 PI-----------TVATYQSLAR-RAHLDELGDR-FGLVIIDEAHH------AGAPSY---RRILEAFPAayRLGLTATP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 317 EqlgleshfaRLRLLDPnRFHDFAQFVEEqnnyrpvadavamllagkrlsddelNTLSDLIGEQDIEPLlqaansdsdna 396
Cdd:COG1061 224 F---------RSDGREI-LLFLFDGIVYE-------------------------YSLKEAIEDGYLAPP----------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 397 esarkelidmlmdrhgtsrvlfrntrngvkgfpkrELHTIKLPLptqyqtaikvsgimgarktQEERARDMLYPEQIYQE 476
Cdd:COG1061 258 -----------------------------------EYYGIRVDL-------------------TDERAEYDALSERLREA 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 477 FEGDtgtwwnfDPRV-EWLMGYLTAHRS-RKVLVICAKAATALQLEQVLREReGIRAAVFHEGMSIVERDRAAAWFGEED 554
Cdd:COG1061 284 LAAD-------AERKdKILRELLREHPDdRKTLVFCSSVDHAEALAELLNEA-GIRAAVVTGDTPKKEREEILEAFRDGE 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 555 SgaQVLLCSEIGSEGRNFQFASNLVMFDLPFNPDLLEQRIGRLDRIGQAHD-------IQIHVPYLEKTAQSVLVRWFHE 627
Cdd:COG1061 356 L--RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdalvydfVGNDVPVLEELAKDLRDLAGYR 433
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 628 GLDAFEHTC----PTGRTIYDQVHGDLIGYLAAPENAEGFDELIKSCREKHDALKAQLEQGRDRLLEIHSNGGEKAQALA 703
Cdd:COG1061 434 VEFLDEEESeelaLLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKE 513
|
....*....
gi 556425441 704 ESIEEQDDD 712
Cdd:COG1061 514 LLLLLALAK 522
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
175-344 |
7.88e-12 |
|
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: 65.66 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 175 LADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEmLRRFN--LRFSLFDDeryAEAQHDADNPFETEQLV 252
Cdd:cd18012 28 LADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEE-AAKFApeLKVLVIHG---TKRKREKLRALEDYDLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 253 ICSLDFVRRSkqrLEHLCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLaeRVPGVLLLTATPeqlgLESHFARL---- 328
Cdd:cd18012 104 ITSYGLLRRD---IELLKEVKFHYLVLDEAQNI---KNPQTKTAKAVKAL--KADHRLALTGTP----IENHLGELwsif 171
|
170
....*....|....*.
gi 556425441 329 RLLDPNRFHDFAQFVE 344
Cdd:cd18012 172 DFLNPGLLGSYKRFKK 187
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
173-350 |
1.11e-11 |
|
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: 65.45 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 173 VLLADEVGLGKTIEA----GMILHQQLLSGAaerVLIVVP--------ETLQhQWLVEMlrrfNLRFSLFDDE-----RY 235
Cdd:cd17993 23 GILADEMGLGKTVQTisflSYLFHSQQQYGP---FLVVVPlstmpawqREFA-KWAPDM----NVIVYLGDIKsrdtiRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 236 AEAQHDADNPFETEQLvICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLVWSEdapSREYMAIEQLaeRVPGVLLLTAT 315
Cdd:cd17993 95 YEFYFSQTKKLKFNVL-LTTYEIILKDKAFLGSI---KWQYLAVDEAHRLKNDE---SLLYEALKEF--KTNNRLLITGT 165
|
170 180 190
....*....|....*....|....*....|....*
gi 556425441 316 PEQLGLESHFARLRLLDPNRFHDFAQFVEEQNNYR 350
Cdd:cd17993 166 PLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQ 200
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
174-345 |
2.73e-11 |
|
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: 64.19 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAER-VLIVVP-ETLQHqWLVEMLRRFNLRFSLFDDERYAEA---QHDADNPFE- 247
Cdd:cd17995 23 ILADEMGLGKTIQSIAFLEHLYQVEGIRGpFLVIAPlSTIPN-WQREFETWTDMNVVVYHGSGESRQiiqQYEMYFKDAq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 248 ---------------TEQLVICSLDFVRRskqrlehlcdAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLA-ERvpgVLL 311
Cdd:cd17995 102 grkkkgvykfdvlitTYEMVIADAEELRK----------IPWRVVVVDEAHRL---KNRNSKLLQGLKKLTlEH---KLL 165
|
170 180 190
....*....|....*....|....*....|....
gi 556425441 312 LTATPEQLGLESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd17995 166 LTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEE 199
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
154-336 |
3.09e-10 |
|
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: 60.91 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 154 LIPHQLN----IAHDVGRRHAprVLLADEVGLGKTIEAgmilhQQLLSGAAERV------LIVVPETLQHQWlVEMLRRF 223
Cdd:cd18006 1 LRPYQLEgvnwLLQCRAEQHG--CILGDEMGLGKTCQT-----ISLLWYLAGRLkllgpfLVLCPLSVLDNW-KEELNRF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 224 --NLRFSLF--DDERYAEAQHD--ADNPFE----TEQLVICSLDFVRRSKqrlehlcdaeWDIMVVDEAHHLvwsEDAPS 293
Cdd:cd18006 73 apDLSVITYmgDKEKRLDLQQDikSTNRFHvlltTYEICLKDASFLKSFP----------WASLVVDEAHRL---KNQNS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556425441 294 REYMAIEQLAerVPGVLLLTATPEQLGLESHFARLRLLDPNRF 336
Cdd:cd18006 140 LLHKTLSEFS--VDFRLLLTGTPIQNSLQELYALLSFIEPNVF 180
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
175-344 |
2.33e-09 |
|
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: 58.90 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 175 LADEVGLGKTIEAGMIL------HQQLLSGAAERVLIVVPETLQHQWLVEMLRRFNlRFSLFDDERYAEAQHDADNP--F 246
Cdd:cd17999 24 LCDDMGLGKTLQTLCILasdhhkRANSFNSENLPSLVVCPPTLVGHWVAEIKKYFP-NAFLKPLAYVGPPQERRRLReqG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 247 ETEQLVICSLDFVRRSkqrLEHLCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLAERvpGVLLLTATPEQ---LGLES 323
Cdd:cd17999 103 EKHNVIVASYDVLRND---IEVLTKIEWNYCVLDEGHII---KNSKTKLSKAVKQLKAN--HRLILSGTPIQnnvLELWS 174
|
170 180
....*....|....*....|.
gi 556425441 324 HFArlrLLDPNRFHDFAQFVE 344
Cdd:cd17999 175 LFD---FLMPGYLGTEKQFQR 192
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
174-345 |
1.12e-08 |
|
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: 56.59 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVE----------------MLRRFNLRFSLFdderYAE 237
Cdd:cd18058 23 ILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREfrtwtemnaivyhgsqISRQMIQQYEMY----YRD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 238 AQhdaDNPFETE---QLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLVwSEDAPSREYMAIEQLAERVpgvlLLTA 314
Cdd:cd18058 99 EQ---GNPLSGIfkfQVVITTFEMILADCPELKKI---NWSCVIIDEAHRLK-NRNCKLLEGLKLMALEHKV----LLTG 167
|
170 180 190
....*....|....*....|....*....|.
gi 556425441 315 TPEQLGLESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd18058 168 TPLQNSVEELFSLLNFLEPSQFPSETTFLEE 198
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
154-318 |
6.05e-08 |
|
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: 54.68 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 154 LIPHQLNIAHDVGRRHAPRV--LLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMLR-RFNLRFSLF 230
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKggILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKwTPGLRVKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 231 DDERYAEAQHDADNPFETEQLVICSLDFVRRSKQRLEHLCDAE--WDIMVVDEAHHLvwsEDAPSREYMAIEQLAERVPg 308
Cdd:cd18001 81 HGTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDHDEfkWDYVILDEGHKI---KNSKTKSAKSLREIPAKNR- 156
|
170
....*....|
gi 556425441 309 vLLLTATPEQ 318
Cdd:cd18001 157 -IILTGTPIQ 165
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
174-318 |
1.49e-07 |
|
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: 52.71 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMIL----HQQLLSGaaeRVLIVVPETLQHQWLVEMLRRF-NLRFSLF--------DDERYAEAQH 240
Cdd:cd18000 23 ILGDEMGLGKTIQIIAFLaalhHSKLGLG---PSLIVCPATVLKQWVKEFHRWWpPFRVVVLhssgsgtgSEEKLGSIER 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 241 DA---DNPFETEQLVICSLDFVRRSKQrleHLCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLaeRVPGVLLLTATPE 317
Cdd:cd18000 100 KSqliRKVVGDGGILITTYEGFRKHKD---LLLNHNWQYVILDEGHKI---RNPDAEITLACKQL--RTPHRLILSGTPI 171
|
.
gi 556425441 318 Q 318
Cdd:cd18000 172 Q 172
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
174-342 |
4.06e-07 |
|
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: 52.00 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMLR----------------RFNLRfslfdDERYAE 237
Cdd:cd18009 26 ILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARftpsvpvllyhgtkeeRERLR-----KKIMKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 238 AQHDADNPfeteqLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLVWSEDAPSREYMAIeQLAERvpgvLLLTATPE 317
Cdd:cd18009 101 EGTLQDFP-----VVVTSYEIAMRDRKALQHY---AWKYLIVDEGHRLKNLNCRLIQELKTF-NSDNR----LLLTGTPL 167
|
170 180
....*....|....*....|....*
gi 556425441 318 QLGLESHFARLRLLDPNRFHDFAQF 342
Cdd:cd18009 168 QNNLSELWSLLNFLLPDVFDDLSSF 192
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
165-333 |
5.03e-07 |
|
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: 51.77 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 165 VGRRHAPR--VLLADEVGLGKTIEAGMILHQQLLSG------AAERVLIVVPETLQHQWLVEMLRrfnlrfsLFDDERYA 236
Cdd:cd18066 17 MGMRVNERfgAILADEMGLGKTLQCISLIWTLLRQGpyggkpVIKRALIVTPGSLVKNWKKEFQK-------WLGSERIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 237 EAQHDADNPFET------EQLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLvwsEDAPSREYMAIEQL-AERvpgV 309
Cdd:cd18066 90 VFTVDQDHKVEEfiasplYSVLIISYEMLLRSLDQISKL---NFDLVICDEGHRL---KNTSIKTTTALTSLsCER---R 160
|
170 180
....*....|....*....|....
gi 556425441 310 LLLTATPEQLGLESHFARLRLLDP 333
Cdd:cd18066 161 IILTGTPIQNDLQEFFALIDFVNP 184
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
173-345 |
7.32e-07 |
|
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: 50.90 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 173 VLLADEVGLGKTIEAGMILHQQLLSGAAE-RVLIVVPETLQHQWLVEmlrrfnlrFSLFDDERYAEAQHDadnpfetEQL 251
Cdd:cd17994 22 TILADEMGLGKTIQTIVFLYSLYKEGHSKgPFLVSAPLSTIINWERE--------FEMWAPDFYVVTYVG-------DHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 252 VICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLvwsEDAPSREYMAIEQLaeRVPGVLLLTATPEQLGLESHFARLRLL 331
Cdd:cd17994 87 LLTSYELISIDQAILGSI---DWAVLVVDEAHRL---KNNQSKFFRILNSY--KIGYKLLLTGTPLQNNLEELFHLLNFL 158
|
170
....*....|....
gi 556425441 332 DPNRFHDFAQFVEE 345
Cdd:cd17994 159 TPERFNNLQGFLEE 172
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
174-347 |
8.33e-07 |
|
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: 51.17 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEA----GMILHQQLLSGAAervLIVVPETLQHQWLVEMLRRF-NLRFSLFDDERYAEAQHDADNPFET 248
Cdd:cd18065 38 ILADEMGLGKTLQTiallGYLKHYRNIPGPH---MVLVPKSTLHNWMNEFKRWVpSLRAVCLIGDKDARAAFIRDVMMPG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 249 E-QLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLVWSEDAPS---REYMAIEQlaervpgvLLLTATPEQLGLESH 324
Cdd:cd18065 115 EwDVCVTSYEMVIKEKSVFKKF---NWRYLVIDEAHRIKNEKSKLSeivREFKTTNR--------LLLTGTPLQNNLHEL 183
|
170 180
....*....|....*....|....*.
gi 556425441 325 FARLRLLDPNRFH---DFAQFVEEQN 347
Cdd:cd18065 184 WALLNFLLPDVFNsadDFDSWFDTKN 209
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
174-365 |
9.42e-07 |
|
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: 51.19 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEA-GMILHQQLLS-------------------GAAERV------LIVVPETLQHQWLVEMLR--RFNL 225
Cdd:cd18070 18 ILADEMGLGKTVEVlALILLHPRPDndldaadddsdemvccpdcLVAETPvsskatLIVCPSAILAQWLDEINRhvPSSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 226 RFSLFD--DERYAEAQHDADNpFETEQLVICSLDFVR---------RSKQRLEH----------LCDAEWDIMVVDEAhH 284
Cdd:cd18070 98 KVLTYQgvKKDGALASPAPEI-LAEYDIVVTTYDVLRtelhyaeanRSNRRRRRqkryeappspLVLVEWWRVCLDEA-Q 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 285 LVWSEDAPSREyMAIEQLAERVPGVlllTATPEQLGLESHFARLRLLDPNRF--HDFAQFVEEQNNYRPVADAVAMLLAG 362
Cdd:cd18070 176 MVESSTSKAAE-MARRLPRVNRWCV---SGTPIQRGLDDLFGLLSFLGVEPFcdSDWWARVLIRPQGRNKAREPLAALLK 251
|
...
gi 556425441 363 KRL 365
Cdd:cd18070 252 ELL 254
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
172-317 |
1.22e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 49.21 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 172 RVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLqhqwLVE-MLRRFNLRFS-------LFDDERYAEAQHDAD 243
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKD----LLEqALEEFKKFLPnyveigeIISGDKKDESVDDNK 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556425441 244 NPFETEQlvicSLDfvRRSKQRLEHLCDAEWDIMVVDEAHHLVwsedAPSreymaIEQLAERVPGVLLL--TATPE 317
Cdd:pfam04851 101 IVVTTIQ----SLY--KALELASLELLPDFFDVIIIDEAHRSG----ASS-----YRNILEYFKPAFLLglTATPE 161
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
174-336 |
1.25e-06 |
|
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: 49.69 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEmLRRF--NLRFSLF---DDERyAEAQHDADNPFE- 247
Cdd:cd17998 23 ILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLRE-FKRWcpSLKVEPYygsQEER-KHLRYDILKGLEd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 248 ------TEQLVICSLD---FVRRSKqrlehlcdaeWDIMVVDEAHHLVWSEDAPSREYMAIeqlaeRVPGVLLLTATPEQ 318
Cdd:cd17998 101 fdvivtTYNLATSNPDdrsFFKRLK----------LNYVVYDEGHMLKNMTSERYRHLMTI-----NANFRLLLTGTPLQ 165
|
170
....*....|....*...
gi 556425441 319 LGLESHFARLRLLDPNRF 336
Cdd:cd17998 166 NNLLELMSLLNFIMPKPF 183
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
174-342 |
1.46e-06 |
|
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: 50.55 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSG-----AAERVLIVVPETLQHQWLVEMLRRFNLRFSLF--------DDERYAEAQH 240
Cdd:cd18067 28 IMADEMGLGKTLQCITLMWTLLRQSpqckpEIDKAIVVSPSSLVKNWANELGKWLGGRLQPLaidggskkEIDRKLVQWA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 241 DADNPFETEQLVICSLDFVRRSkqrLEHLCDAEWDIMVVDEAHHLVWSEdapSREYMAIEQLaeRVPGVLLLTATPEQLG 320
Cdd:cd18067 108 SQQGRRVSTPVLIISYETFRLH---VEVLQKGEVGLVICDEGHRLKNSD---NQTYQALDSL--NTQRRVLLSGTPIQND 179
|
170 180
....*....|....*....|..
gi 556425441 321 LESHFARLRLLDPNRFHDFAQF 342
Cdd:cd18067 180 LSEYFSLVNFVNPGILGTAAEF 201
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
173-342 |
2.03e-06 |
|
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: 50.07 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 173 VLLADEVGLGKTIEA----GMILH-----------------QQLLSGAAERVLIVVPETLQHQWLVEMLRRFNLRFSLF- 230
Cdd:cd18005 22 GILGDDMGLGKTVQViaflAAVLGktgtrrdrennrprfkkKPPASSAKKPVLIVAPLSVLYNWKDELDTWGHFEVGVYh 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 231 ----DDERYAEAQHDAdnpfetEQLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLvwsEDAPSREYMAIEQL-AER 305
Cdd:cd18005 102 gsrkDDELEGRLKAGR------LEVVVTTYDTLRRCIDSLNSI---NWSAVIADEAHRI---KNPKSKLTQAMKELkCKV 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 556425441 306 VPGvllLTATPEQLGLESHFARLRLLDPNRFHDFAQF 342
Cdd:cd18005 170 RIG---LTGTLLQNNMKELWCLLDWAVPGALGSRSQF 203
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
174-345 |
2.19e-06 |
|
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: 49.64 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMLRRFNLRFSLFDDER------------YAEAQHD 241
Cdd:cd18059 23 ILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYHGSQasrrtiqlyemyFKDPQGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 242 ADNPFETEQLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLVwSEDAPSREYMAIEQLAERVpgvlLLTATPEQLGL 321
Cdd:cd18059 103 VIKGSYKFHAIITTFEMILTDCPELRNI---PWRCVVIDEAHRLK-NRNCKLLEGLKMMDLEHKV----LLTGTPLQNTV 174
|
170 180
....*....|....*....|....
gi 556425441 322 ESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd18059 175 EELFSLLHFLEPSRFPSETTFMQE 198
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
174-347 |
2.71e-06 |
|
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: 49.66 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEA----GMILHQQLLSGAAervLIVVPETLQHQWLVEMLRRFNLRFS---LFDDERYAEAQHDADNPF 246
Cdd:cd18064 38 ILADEMGLGKTLQTisllGYMKHYRNIPGPH---MVLVPKSTLHNWMAEFKRWVPTLRAvclIGDKDQRAAFVRDVLLPG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 247 ETEqLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHlVWSEDAPSREYMAIEQLAERvpgvLLLTATPEQLGLESHFA 326
Cdd:cd18064 115 EWD-VCVTSYEMLIKEKSVFKKF---NWRYLVIDEAHR-IKNEKSKLSEIVREFKTTNR----LLLTGTPLQNNLHELWA 185
|
170 180
....*....|....*....|....
gi 556425441 327 RLRLLDPNRFH---DFAQFVEEQN 347
Cdd:cd18064 186 LLNFLLPDVFNsaeDFDSWFDTNN 209
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
174-345 |
3.57e-06 |
|
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: 49.23 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVEMLRRFNLRFSLFD------------DERYAEAQHD 241
Cdd:cd18061 23 ILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYHgslisrqmiqqyEMYFRDSQGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 242 ADNPFETEQLVICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLVwSEDAPSREYMAIEQLAERVpgvlLLTATPEQLGL 321
Cdd:cd18061 103 IIRGAYRFQAIITTFEMILGGCPELNAI---DWRCVIIDEAHRLK-NKNCKLLEGLKLMNLEHKV----LLTGTPLQNTV 174
|
170 180
....*....|....*....|....
gi 556425441 322 ESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd18061 175 EELFSLLHFLEPLRFPSESTFMQE 198
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
174-345 |
4.35e-06 |
|
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: 48.90 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVPETLQHQWLVE--------------------MLRRFNLrFSLFDDE 233
Cdd:cd18060 23 ILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREfntwtemntivyhgslasrqMIQQYEM-YCKDSRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 234 RYAEAQHDADNPFETEQLVICSLDFVRrskqrlehlcDAEWDIMVVDEAHHLVwSEDAPSREYMAIEQLAERVpgvlLLT 313
Cdd:cd18060 102 RLIPGAYKFDALITTFEMILSDCPELR----------EIEWRCVIIDEAHRLK-NRNCKLLDSLKHMDLEHKV----LLT 166
|
170 180 190
....*....|....*....|....*....|..
gi 556425441 314 ATPEQLGLESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd18060 167 GTPLQNTVEELFSLLHFLEPSQFPSESEFLKD 198
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
174-378 |
4.70e-06 |
|
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: 48.91 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAE-RVLIVVPETLQHQWLvemlRRFNLRFSLFDDERYAEAQHDA----DNPFET 248
Cdd:cd18057 23 ILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWE----REFEMWAPDFYVVTYTGDKESRsvirENEFSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 249 EQLVICSLDFVRRSKQRLE---H---------------LCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEqlAERVPGVL 310
Cdd:cd18057 99 EDNAIRSGKKVFRMKKEAQikfHvlltsyelitidqaiLGSIEWACLVVDEAHRL---KNNQSKFFRVLN--SYKIDYKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556425441 311 LLTATPEQLGLESHFARLRLLDPNRFHDFAQFVEEqnnyrpVADAVamllagkrlSDDELNTLSDLIG 378
Cdd:cd18057 174 LLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEE------FADIS---------KEDQIKKLHDLLG 226
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
174-347 |
5.23e-06 |
|
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: 48.47 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEA----GMILHQQLLSGAAervLIVVPETLQHQWLVEMLR---RFNLRFSLFDDERYAEAQHDA--DN 244
Cdd:cd17997 26 ILADEMGLGKTLQTisllGYLKHYKNINGPH---LIIVPKSTLDNWMREFKRwcpSLRVVVLIGDKEERADIIRDVllPG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 245 PFEteqLVICSLDFVRRSKQrleHLCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLAERvpGVLLLTATPEQLGLESH 324
Cdd:cd17997 103 KFD---VCITSYEMVIKEKT---VLKKFNWRYIIIDEAHRI---KNEKSKLSQIVRLFNSR--NRLLLTGTPLQNNLHEL 171
|
170 180
....*....|....*....|....*.
gi 556425441 325 FARLRLLDPNRF---HDFAQFVEEQN 347
Cdd:cd17997 172 WALLNFLLPDVFtssEDFDEWFNVNN 197
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
174-344 |
7.10e-06 |
|
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: 48.27 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAgmilhQQLLSGAAER------VLIVVPETLQHQWLVEMlRRFNLRFSLFD-----DERYA------ 236
Cdd:cd18002 23 ILADEMGLGKTVQS-----IAVLAHLAEEhniwgpFLVIAPASTLHNWQQEI-SRFVPQFKVLPywgnpKDRKVlrkfwd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 237 -EAQHDADNPFE----TEQLVICSLDFVRRSKqrlehlcdaeWDIMVVDEAHHLvwsEDAPSREYMAIEQLAERvpGVLL 311
Cdd:cd18002 97 rKNLYTRDAPFHvvitSYQLVVQDEKYFQRVK----------WQYMVLDEAQAI---KSSSSSRWKTLLSFHCR--NRLL 161
|
170 180 190
....*....|....*....|....*....|...
gi 556425441 312 LTATPEQLGLESHFARLRLLDPNRFHDFAQFVE 344
Cdd:cd18002 162 LTGTPIQNSMAELWALLHFIMPTLFDSHDEFNE 194
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
494-602 |
7.85e-06 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 46.35 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 494 LMGYLTAHRSRKVLVICAKAATALQLEQVLREReGIRAAVFHEGMSIVERDRAAAWFGEEDSGaqVLLCSEIGSEGRNFQ 573
Cdd:cd18787 18 LLLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL-GIKVAALHGDLSQEERERALKKFRSGKVR--VLVATDVAARGLDIP 94
|
90 100
....*....|....*....|....*....
gi 556425441 574 FASNLVMFDLPFNPDLLEQRIGRLDRIGQ 602
Cdd:cd18787 95 GVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
154-342 |
8.98e-06 |
|
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: 48.06 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 154 LIPHQL--------NIAHDVGRRHAPR-VLLADEVGLGKTIEAGMILH--QQLLSGAAeRVLIVVPETLQHQWLVEmLRR 222
Cdd:cd18007 1 LKPHQVegvrflwsNLVGTDVGSDEGGgCILAHTMGLGKTLQVITFLHtyLAAAPRRS-RPLVLCPASTLYNWEDE-FKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 223 FNLRFSL-FDDERYAEAQHDADNPFET---------------EQLV--ICSLDFVRRSKQRLEH-LCDAEWDIMVVDEAH 283
Cdd:cd18007 79 WLPPDLRpLLVLVSLSASKRADARLRKinkwhkeggvlligyELFRnlASNATTDPRLKQEFIAaLLDPGPDLLVLDEGH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556425441 284 HLvwsEDAPSREYMAIEQLaeRVPGVLLLTATPEQLGLESHFARLRLLDPNRFHDFAQF 342
Cdd:cd18007 159 RL---KNEKSQLSKALSKV--KTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEF 212
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
180-316 |
2.37e-05 |
|
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: 45.37 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 180 GLGKTIEagMILHQQLLSgaAERVLIVVPET-LQHQWlVEMLRRFNLRFSLFddERYAEAQHDadnpFETEQLVICSLDF 258
Cdd:cd17926 28 GSGKTLT--ALALIAYLK--ELRTLIVVPTDaLLDQW-KERFEDFLGDSSIG--LIGGGKKKD----FDDANVVVATYQS 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 259 VRRSKQRLEHLCDaEWDIMVVDEAHHLvwsedaPSREYmaiEQLAERVPG--VLLLTATP 316
Cdd:cd17926 97 LSNLAEEEKDLFD-QFGLLIVDEAHHL------PAKTF---SEILKELNAkyRLGLTATP 146
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
174-345 |
3.59e-05 |
|
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: 46.21 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAE-RVLIVVPETLQHQWLVEmlrrfnlrFSLFDDERYAE---AQHDA-----DN 244
Cdd:cd18056 23 ILADEMGLGKTVQTAVFLYSLYKEGHSKgPFLVSAPLSTIINWERE--------FEMWAPDMYVVtyvGDKDSraiirEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 245 PFETEQLVICSLDFVRRSKQR------------------LEHLCDAEWDIMVVDEAHHLvwsEDAPSREYMAIEQLAerV 306
Cdd:cd18056 95 EFSFEDNAIRGGKKASRMKKEasvkfhvlltsyelitidMAILGSIDWACLIVDEAHRL---KNNQSKFFRVLNGYS--L 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 556425441 307 PGVLLLTATPEQLGLESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd18056 170 QHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEE 208
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
174-350 |
4.93e-05 |
|
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: 45.81 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEA----GMILHQQLLSGAaerVLIVVPETLQHQWLVEM---LRRFNLRFSLFD-DERYAEAQHDADNP 245
Cdd:cd18053 43 ILADEMGLGKTIQTisflNYLFHEHQLYGP---FLLVVPLSTLTSWQREIqtwAPQMNAVVYLGDiNSRNMIRTHEWMHP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 246 fETEQL----VICSLDFVRRSKQRLEHLcdaEWDIMVVDEAHHLVwSEDAPSREYMAIEQLAERvpgvLLLTATPEQLGL 321
Cdd:cd18053 120 -QTKRLkfniLLTTYEILLKDKSFLGGL---NWAFIGVDEAHRLK-NDDSLLYKTLIDFKSNHR----LLITGTPLQNSL 190
|
170 180
....*....|....*....|....*....
gi 556425441 322 ESHFARLRLLDPNRFHDFAQFVEEQNNYR 350
Cdd:cd18053 191 KELWSLLHFIMPEKFSSWEDFEEEHGKGR 219
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
166-317 |
7.80e-05 |
|
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: 44.09 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 166 GRRhapRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIVVP-ETLQHQwLVEMLRRFNLRFSLFDDERyaeaqhDADN 244
Cdd:cd18032 19 GQR---RALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHrEELLEQ-AERSFKEVLPDGSFGNLKG------GKKK 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425441 245 PFETEQlVICSLDFVRRSKqRLEHLCDAEWDIMVVDEAHHlvwsedAPSREYMAIeqLAERVPGVLL-LTATPE 317
Cdd:cd18032 89 PDDARV-VFATVQTLNKRK-RLEKFPPDYFDLIIIDEAHH------AIASSYRKI--LEYFEPAFLLgLTATPE 152
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
273-345 |
2.39e-04 |
|
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: 43.85 E-value: 2.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556425441 273 EWDIMVVDEAHHLvwsEDAPSREYMAIEQLaeRVPGVLLLTATPEQLGLESHFARLRLLDPNRFHDFAQFVEE 345
Cdd:cd18055 141 RWACLVVDEAHRL---KNNQSKFFRVLNGY--KIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEE 208
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
174-342 |
1.41e-03 |
|
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: 41.41 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMILHQQLLSGAAE---RVLIVVPETLQHQWLVEM------LRRFNlRFSLFDDERYAEAQ---HD 241
Cdd:cd18068 32 ILAHCMGLGKTLQVVTFLHTVLLCEKLEnfsRVLVVCPLNTVLNWLNEFekwqegLKDEE-KIEVNELATYKRPQersYK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 242 ADNPFETEQLVICSLDFVR----------RSKQR---LEHLCDAEWDIMVVDEAHHLVWSEDAPSREYMAIeqlaeRVPG 308
Cdd:cd18068 111 LQRWQEEGGVMIIGYDMYRilaqernvksREKLKeifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSI-----RTKR 185
|
170 180 190
....*....|....*....|....*....|....
gi 556425441 309 VLLLTATPEQLGLESHFARLRLLDPNRFHDFAQF 342
Cdd:cd18068 186 RIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEF 219
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
174-344 |
1.62e-03 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 42.48 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 174 LLADEVGLGKTIEAGMI---LHQqlLSGAAERVLIVVPETLQHQWLVEmLRRFN--LRFSLF---DDERyaeaQHDADNP 245
Cdd:PLN03142 192 ILADEMGLGKTLQTISLlgyLHE--YRGITGPHMVVAPKSTLGNWMNE-IRRFCpvLRAVKFhgnPEER----AHQREEL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 246 FETEQLVICSLDFVRRSKQRlEHLCDAEWDIMVVDEAHHLVwSEDAPSREYMAIEQLAERvpgvLLLTATPEQLGLESHF 325
Cdd:PLN03142 265 LVAGKFDVCVTSFEMAIKEK-TALKRFSWRYIIIDEAHRIK-NENSLLSKTMRLFSTNYR----LLITGTPLQNNLHELW 338
|
170
....*....|....*....
gi 556425441 326 ARLRLLDPNRFHDFAQFVE 344
Cdd:PLN03142 339 ALLNFLLPEIFSSAETFDE 357
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
174-221 |
2.62e-03 |
|
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: 40.73 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556425441 174 LLADEVGLGKTIEA-GMIL--HQQLLSGAAERV---------------LIVVPETLQHQWLVEMLR 221
Cdd:cd18008 18 ILADEMGLGKTIQAlALILatRPQDPKIPEELEenssdpkklylskttLIVVPLSLLSQWKDEIEK 83
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
178-332 |
5.65e-03 |
|
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: 39.26 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 178 EVGLGKTIEAGMILHQQLLSGAAERVLIVVPETL-QHQWLVEMLR---RFNLRFSLFDD---ERYAEAQHDADNPFETEQ 250
Cdd:cd18013 23 DMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVaRSTWPDEVEKwnhLRNLTVSVAVGterQRSKAANTPADLYVINRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425441 251 LVIcslDFVRRSKQRLEhlcdaeWDIMVVDEAHHLvwsEDAPSREYMAIEQLAERVPGVLLLTATPEQLGLESHFARLRL 330
Cdd:cd18013 103 NLK---WLVNKSGDPWP------FDMVVIDELSSF---KSPRSKRFKALRKVRPVIKRLIGLTGTPSPNGLMDLWAQIAL 170
|
..
gi 556425441 331 LD 332
Cdd:cd18013 171 LD 172
|
|
| |
