|
Name |
Accession |
Description |
Interval |
E-value |
| DISARM_DrmD |
NF038317 |
DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component ... |
8-906 |
2.42e-73 |
|
DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase.
Pssm-ID: 468471 [Multi-domain] Cd Length: 1023 Bit Score: 261.32 E-value: 2.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 8 PGSLIHARGREWIV----QPGSVPPLLRLRPLSGTEEeGAL-----IHIDLEPG---IESAHfpPPDPSQEG----SQGE 71
Cdd:NF038317 4 PGQLVEVRGRQWVVsdvqLPRSPADQQHLVTLQSLDD-DALgeeldVIWELEPGarvLERAG--LPEVTEGGfddpERLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 72 AILlsDALRMALRRGAG------PFRSfgNIAVEPrtYQLVPLLMALRLDPVRLLIADDVGIGKTIEAALIARELQDRGE 145
Cdd:NF038317 81 AFL--DAVRWGAVTSADrrllqaPFRS--GISIED--YQLEPLVRALDMPRVNLLIADDVGLGKTIEAGLVIQELLLRHR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 146 IQRMAILCPPHLVEQWVRELNDRFHLHAVAVTATSAARL--ERGIpvGESLFQVHPVTVVSLDYIKSERHRHDFIRACPE 223
Cdd:NF038317 155 ARRVLIVCPASLQEKWRDEMREKFGLDFRIVDSEYVAQLrrERGL--HANPWTSFPRLIVSMDWLRGERAQRLLRDVLPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 224 F---------VIVDEAHTCVSAGQGRQ----LRFELLRALAANeARHLVLLTATPHSGDQDTFYSLLGLLKPE-FAALAt 289
Cdd:NF038317 233 HadtprafdlLIVDEAHNVAPASPSKYavdsQRTRLIRDLAPH-FEHRLFLSATPHNGYSESFTALLELLDPQrFARGV- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 290 asgDTKERLRHQLAlhfVQRRRPDIDEWQDGSIFPQRETAELTYRLGGLWENFFQDVLDYCrEVVQRAGGDERSQRLSFW 369
Cdd:NF038317 311 ---PPDEKQLDEVM---VRRLKSDLVDRDGSPRFPERELEALPVDYSADEREIHELLDEYT-ELRRKRLAGKRGRRAADF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 370 GTLALMRCVASSPAA-------AVQALRTRLLAEQVEQAPEEILGPLFDGTEDALS--------EDDVVPAADIGDPAL- 433
Cdd:NF038317 384 VTLLLKKRLFSSPAAfartlevHRATLERGAARGGPLSDDERLLRDDVLDDEEDYAddelleeaEDEALEEASELSPPLt 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 434 ---LDLLNKAETLAGEES---DPKLRLLGRHLKQ-LIDDGFNP----VVFCRYIATARYLHDHLAGR-FRGVTVDVVTGE 501
Cdd:NF038317 464 aeeRALLERLRAWAERAEarpDSKARALIDWLRAnLRPGGRWTnervIVFTEYRDTLRWLVELLAAEgYGGDRLALLHGG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 502 FPAAERERRVDAL----GEAERRLLIATDCLSEGINLQENLDAVVHYDLSWNPTRHEQREGRVDRFGQTSPKVRatlIY- 576
Cdd:NF038317 544 MDDDERERIKAAFqadpSEHPVRILLATDAASEGIDLQNHCHRLIHYDIPWNPNRLEQRNGRIDRHGQRADPVL---IWh 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 577 ------GANNPVDGAVLQVILRKAEKIRQELGvpvplpdddhTLTQALMKAVmlrsERAggpqrsfdfdqyPESRALDVR 650
Cdd:NF038317 621 fvgkgtEGAAEGDLEFLDRLARKVATIREDLG----------SVNPVIADQV----ERL------------LLGRRRDLD 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 651 WTDLAEKAKKNRTVFAQRRLRP--ADVLPEWERMRAVLG-SSDDVKRFATQAMaRLGAGLSLRARGATAP------ISAL 721
Cdd:NF038317 675 TEAAEIEAAKRRELAAERELREqlERLHEQLEESREELHlTPANIRRVVDTAL-ELAGQPPLVPVGDPGPdgrvfeVPAL 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 722 P---AALRERLAAEGVDGDLR-IDFNqPPASRCR----FIHRSHPLIAtLADELLERSLMAETHDgqqlatLGRIGVWRS 793
Cdd:NF038317 754 SgswARALDGLRHPLHTGQIRpITFD-PEVAKGRddvvLVHLNHPLVQ-MSLRLLRAAVWSDDKP------LHRVTAVVV 825
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 794 P--AVQSVTSVLLLRLrhqISTtreGRNQTLLVEEALPVA---WQGRTVPVEIQGDqLLAWLEA--PAQGNLPDVVRQRE 866
Cdd:NF038317 826 PddGLEEPAVAALSRL---VLV---GGDGARLHEELLLAGgwlRDGRFRRLEGVTD-VEALLDAalPSGRPAPPAVRDRL 898
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 2792345535 867 MHNLLETLQQRQEQLEQLADDQAERL---LADhRRVREAADAR 906
Cdd:NF038317 899 AERWPRLRERLEEALEARARDRLDALertLAD-RGEAEAQRIR 940
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
100-309 |
2.14e-59 |
|
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: 201.75 E-value: 2.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 100 PRTYQLVPLLMALRLDPVRLLIADDVGIGKTIEAALIARELQDRGEIQRMAILCPPHLVEQWVRELNDRFHLHAVAVTAT 179
Cdd:cd18011 1 PLPHQIDAVLRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 180 SAARLERGIpvgESLFQVHPVTVVSLDYIKSERHR-HDFIRACPEFVIVDEAHTC-VSAGQGRQLRFELLRALAANeARH 257
Cdd:cd18011 81 TAAQLRRLI---GNPFEEFPIVIVSLDLLKRSEERrGLLLSEEWDLVVVDEAHKLrNSGGGKETKRYKLGRLLAKR-ARH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792345535 258 LVLLTATPHSGDQDTFYSLLGLLKPEFAAlATASGDTKERLRHQLALHFVQR 309
Cdd:cd18011 157 VLLLTATPHNGKEEDFRALLSLLDPGRFA-VLGRFLRLDGLREVLAKVLLRR 207
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
8-602 |
2.39e-57 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 210.08 E-value: 2.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 8 PGSLIHARGREWIVQPGSVPPLLRLRPLSGTEEEGALIHIDLEPGIESAHFPPPDPSQEGSQGEAILLSDALRMALRRGA 87
Cdd:COG0553 149 LLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 88 GPFRSFG-NIAVEPRTYQLVPLLMALRLD--PVRLLIADDVGIGKTIEAALIARELQDRGEIQRMAILCPPHLVEQWVRE 164
Cdd:COG0553 229 EALESLPaGLKATLRPYQLEGAAWLLFLRrlGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 165 LNdRFHLHAVAVTATSAARLERGIpvgeSLFQVHPVTVVSLDYIKseRHRHDFIRACPEFVIVDEAHTCVSAgqgRQLRF 244
Cdd:COG0553 309 LA-KFAPGLRVLVLDGTRERAKGA----NPFEDADLVITSYGLLR--RDIELLAAVDWDLVILDEAQHIKNP---ATKRA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 245 ELLRALAaneARHLVLLTATPHSGDQDTFYSLLGLLKPEF------------AALATASGDTKERLRHQLALHFVQRRRP 312
Cdd:COG0553 379 KAVRALK---ARHRLALTGTPVENRLEELWSLLDFLNPGLlgslkafrerfaRPIEKGDEEALERLRRLLRPFLLRRTKE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 313 DIdewqdGSIFPQRETAELTYRLGGLWENFFQDVLDYCREVVQRAGGDERsqRLSFWGTLALMRCVASSPAaavqalrtr 392
Cdd:COG0553 456 DV-----LKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRR--RGLILAALTRLRQICSHPA--------- 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 393 llaeqveqapeeilgpLFDGTEDALSEDdvvpaadigdpalldllnkaetlageesDPKLRLLGRHLKQLIDDGFNPVVF 472
Cdd:COG0553 520 ----------------LLLEEGAELSGR----------------------------SAKLEALLELLEELLAEGEKVLVF 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 473 CRYIATARYLHDHLAGrfRGVTVDVVTGEFPAAERERRVDAL--GEAERRLLIATDCLSEGINLQEnLDAVVHYDLSWNP 550
Cdd:COG0553 556 SQFTDTLDLLEERLEE--RGIEYAYLHGGTSAEERDELVDRFqeGPEAPVFLISLKAGGEGLNLTA-ADHVIHYDLWWNP 632
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2792345535 551 TRHEQREGRVDRFGQTSPkVRATLIYgANNPVDGAVLQVILRKAEKIRQELG 602
Cdd:COG0553 633 AVEEQAIDRAHRIGQTRD-VQVYKLV-AEGTIEEKILELLEEKRALAESVLG 682
|
|
| DpdE |
NF041062 |
protein DpdE; |
115-565 |
7.07e-37 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 150.51 E-value: 7.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 115 DPV-RLLIADDVGIGKTIEAALIARE-LQDRGEiQRMAILCPPHLVEQWVRELNDRFHLHAvavtatsaarlergipvge 192
Cdd:NF041062 168 DPVqRYLLADEVGLGKTIEAGLVIRQhLLDNPD-ARVLVLVPDALVRQWRRELRDKFFLDD------------------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 193 slFQVHPVTVVSLDYIKSERHRHDfiraCPEFVIVDEAH----TCVSAGQGRQLRFELLRALAANEARhLVLLTATPHSG 268
Cdd:NF041062 228 --FPGARVRVLSHEEPERWEPLLD----APDLLVVDEAHqlarLAWSGDPPERARYRELAALAHAAPR-LLLLSATPVLG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 269 DQDTFYSLLGLLKPEFAALatasgDTKERLRHQLAlhfvQRRRPdidewqdGSIF----PQRETAELTYRLGGLWENFFQ 344
Cdd:NF041062 301 NEETFLALLHLLDPDLYPL-----DDLEAFRERLE----EREEL-------GRLVlgldPDNPNFLLRQALDELRALFPE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 345 DVL-----DYCREVVQRAG---GDERSQRLS------------------------------FWGTLALMRCVASSPA--A 384
Cdd:NF041062 365 DEElqelaEELLPLLDEFDdeePEERARAVSalrahisetyrlhrrmirnrrssvlgadylVPGRAGPRVLVWESPAreA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 385 AVQAL-----RTRLLAEQVEQAPEEILGP----LFDGTEDALSEDDVVPAADIGDPALLDLLNKAETL------AGEESD 449
Cdd:NF041062 445 ADEALedwreEAALLDAESDPAARAAYARalawLVARLGGPDDLAALLRWRLRGDAASADLAGERELLealiaaLEDEAK 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 450 PK--LRLLGRHLKQLIDDGFNPVVFCRYIATARYLHDHLAgRFRGVTVDVVTGEFPAAERERRVDA-LGEAERRLLIATD 526
Cdd:NF041062 525 DAdlLAALADWLLPLLRGSGKAVVFCGDGSLADHLAAALA-RLGAGSVERHLSGQGADQAERAVRAfRQDPSARVLVCDR 603
|
490 500 510
....*....|....*....|....*....|....*....
gi 2792345535 527 CLSEGINLQENlDAVVHYDLSWNPTRHEQREGRVDRFGQ 565
Cdd:NF041062 604 SGEEGLNLQGA-DRLVHLDLPWSPNRLEQRIGRLDRYAS 641
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
449-568 |
6.24e-31 |
|
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: 118.35 E-value: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 449 DPKLRLLGRHLKQLIDDGFNPVVFCRYIATARYLHDHLagRFRGVTVDVVTGEFPAAERERRVDAL--GEAERRLLIATD 526
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEAL--RERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTK 87
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2792345535 527 CLSEGINLQEnLDAVVHYDLSWNPTRHEQREGRVDRFGQTSP 568
Cdd:cd18793 88 AGGVGLNLTA-ANRVILYDPWWNPAVEEQAIDRAHRIGQKKP 128
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
451-564 |
1.26e-18 |
|
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: 82.26 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 451 KLRLLGRHLKQLIDDgfNPVVFCRYIATARYlhDHLAGRfRGVTVDVVTGEFPAAERERRVDALGEAERRLLIATDCLSE 530
Cdd:pfam00271 2 KLEALLELLKKERGG--KVLIFSQTKKTLEA--ELLLEK-EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|....
gi 2792345535 531 GINLQeNLDAVVHYDLSWNPTRHEQREGRVDRFG 564
Cdd:pfam00271 77 GLDLP-DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
99-280 |
3.71e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 81.00 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 99 EPRTYQL--VPLLMALRLDpvrLLIADDVGIGKTIEAALIARELQDRGEIQRMAILCP-PHLVEQWVRELNDRFHLHAVA 175
Cdd:smart00487 8 PLRPYQKeaIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 176 VTAtsaarLERGIPVGESLFQVH----PVTVVSLDYIKSERHRHDFIRACPEFVIVDEAHTCVSAGQGRQLRfELLRALa 251
Cdd:smart00487 85 VVG-----LYGGDSKREQLRKLEsgktDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLE-KLLKLL- 157
|
170 180
....*....|....*....|....*....
gi 2792345535 252 aNEARHLVLLTATPHSGDQDTFYSLLGLL 280
Cdd:smart00487 158 -PKNVQLLLLSATPPEEIENLLELFLNDP 185
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
97-733 |
4.77e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 85.46 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 97 AVEPRTYQ---LVPLLMALRLDPVRLLIADDVGIGKTIEAALIARELQdrgEIQRMAILCP-PHLVEQWVRELNDRFHLH 172
Cdd:COG1061 78 SFELRPYQqeaLEALLAALERGGGRGLVVAPTGTGKTVLALALAAELL---RGKRVLVLVPrRELLEQWAEELRRFLGDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 173 AVavtatsaarlergipVGESLFQVHPVTVVSLDYIKSERHRHDFIRACPeFVIVDEAHTCvSAGQGRQLrfellraLAA 252
Cdd:COG1061 155 LA---------------GGGKKDSDAPITVATYQSLARRAHLDELGDRFG-LVIIDEAHHA-GAPSYRRI-------LEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 253 NEARHLVLLTATPHSGDQdtfysllgllkpefaalatasgdtkerlrhqlalhfvqrrRPDIDEWQDGSIFpqretaELT 332
Cdd:COG1061 211 FPAAYRLGLTATPFRSDG----------------------------------------REILLFLFDGIVY------EYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 333 YRlgglwenffqdvldycrevvqraggdersqrlsfwgtlalmrcvasspaaavQALRTRLLAEqveqapeeilgPLFDG 412
Cdd:COG1061 245 LK----------------------------------------------------EAIEDGYLAP-----------PEYYG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 413 TEDALSEDDVvpAADIGDPALLDLLNKAETLageesdpKLRLLGRHLKQLIDDGfNPVVFCRYIATARYLHDHLagRFRG 492
Cdd:COG1061 262 IRVDLTDERA--EYDALSERLREALAADAER-------KDKILRELLREHPDDR-KTLVFCSSVDHAEALAELL--NEAG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 493 VTVDVVTGEFPAAERERRVDALGEAERRLLIATDCLSEGINLQEnLDAVVHYDLSWNPTRHEQREGRVDRfgQTSPKVRA 572
Cdd:COG1061 330 IRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPR-LDVAILLRPTGSPREFIQRLGRGLR--PAPGKEDA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 573 TLIYGANNPVDgavlqVILRKAEKIRQELGVPVPLPDDDHTLTQALMKAVMLRSERAGG-PQRSFDFDQYPESRALDVRW 651
Cdd:COG1061 407 LVYDFVGNDVP-----VLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGElEEELLEELELLEDALLLVLA 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 652 TDLAEKAKKNRTVFAQRRLRPADVLPEWERMRAVLGSSDDVKRFATQAMARLGAGLSLRARGATAPISALPAALRERLAA 731
Cdd:COG1061 482 ELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKELLR 561
|
..
gi 2792345535 732 EG 733
Cdd:COG1061 562 AA 563
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
100-284 |
4.76e-15 |
|
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: 74.14 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 100 PRTYQLVPL--LMALRLDPVRLLIADDVGIGKTIEA-ALIARELQDRGEIQRMAILCPPHLVEQWVRELNDRF-HLHAVA 175
Cdd:cd17919 1 LRPYQLEGLnfLLELYENGPGGILADEMGLGKTLQAiAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 176 VTATSAARLERGIPVGESLFQVhpvTVVSLDYIksERHRHDFIRACPEFVIVDEAHtCVSAGQGRqlRFELLRALAANea 255
Cdd:cd17919 81 YHGSQRERAQIRAKEKLDKFDV---VLTTYETL--RRDKASLRKFRWDLVVVDEAH-RLKNPKSQ--LSKALKALRAK-- 150
|
170 180
....*....|....*....|....*....
gi 2792345535 256 rHLVLLTATPHSGDQDTFYSLLGLLKPEF 284
Cdd:cd17919 151 -RRLLLTGTPLQNNLEELWALLDFLDPPF 178
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
480-564 |
1.97e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.16 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 480 RYLHDHLagRFRGVTVDVVTGEFPAAERERRVDALGEAERRLLIATDCLSEGINLQeNLDAVVHYDLSWNPTRHEQREGR 559
Cdd:smart00490 1 EELAELL--KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLP-GVDLVIIYDLPWSPASYIQRIGR 77
|
....*
gi 2792345535 560 VDRFG 564
Cdd:smart00490 78 AGRAG 82
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
447-566 |
8.00e-14 |
|
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: 69.07 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 447 ESDPKLRLLGRHLKQLIDDGfNPVVFCRYIATARYLHDHLagRFRGVTVDVVTGEFPAAERERRVDALGEAERRLLIATD 526
Cdd:cd18787 9 EEEEKKLLLLLLLLEKLKPG-KAIIFVNTKKRVDRLAELL--EELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2792345535 527 CLSEGINLqENLDAVVHYDLswnPTRHEQ---REGRVDRFGQT 566
Cdd:cd18787 86 VAARGLDI-PGVDHVINYDL---PRDAEDyvhRIGRTGRAGRK 124
|
|
| PRK04914 |
PRK04914 |
RNA polymerase-associated protein RapA; |
118-283 |
7.55e-11 |
|
RNA polymerase-associated protein RapA;
Pssm-ID: 235319 [Multi-domain] Cd Length: 956 Bit Score: 66.40 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 118 RLLIADDVGIGKTIEAALIARELQDRGEIQRMAILCPPHLVEQWVRELNDRFHLHavaVTATSAARLERGIPVGESLFQV 197
Cdd:PRK04914 171 RVLLADEVGLGKTIEAGMIIHQQLLTGRAERVLILVPETLQHQWLVEMLRRFNLR---FSLFDEERYAEAQHDADNPFET 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 198 HPVTVVSLDYIKSERHRHDFIRACpEF--VIVDEAHTCV-SAGQGRQlRFELLRALAAnEARHLVLLTATPHSGDQDTFY 274
Cdd:PRK04914 248 EQLVICSLDFLRRNKQRLEQALAA-EWdlLVVDEAHHLVwSEEAPSR-EYQVVEQLAE-VIPGVLLLTATPEQLGQESHF 324
|
....*....
gi 2792345535 275 SLLGLLKPE 283
Cdd:PRK04914 325 ARLRLLDPD 333
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
451-566 |
1.23e-09 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 61.32 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 451 KLRLLGRHLKQliDDGFNPVVFCRYIATARYLHDHLagRFRGVTVDVVTGEFPAAERERRVDALGEAERRLLIATDCLSE 530
Cdd:COG0513 228 KLELLRRLLRD--EDPERAIVFCNTKRGADRLAEKL--QKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
|
90 100 110
....*....|....*....|....*....|....*....
gi 2792345535 531 GINLqENLDAVVHYDLswnPTRHEQ---REGRVDRFGQT 566
Cdd:COG0513 304 GIDI-DDVSHVINYDL---PEDPEDyvhRIGRTGRAGAE 338
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
120-282 |
3.59e-09 |
|
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: 58.45 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 120 LIADDVGIGKTIEA-----ALIARELQDRGEIQRMAILCPPHLVEQWVRE----LNDRFhlhAVAVTATSAARLERGIPV 190
Cdd:cd18004 28 ILADEMGLGKTLQAialvwTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEfdkwLGLRR---IKVVTADGNAKDVKASLD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 191 GESLFQVHPVTVVSldYIKSERHRHDFIRA-CPEFVIVDEAHTCVSAGQgrqlrfELLRALAANEARHLVLLTATPHSGD 269
Cdd:cd18004 105 FFSSASTYPVLIIS--YETLRRHAEKLSKKiSIDLLICDEGHRLKNSES------KTTKALNSLPCRRRLLLTGTPIQND 176
|
170
....*....|...
gi 2792345535 270 QDTFYSLLGLLKP 282
Cdd:cd18004 177 LDEFFALVDFVNP 189
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
429-602 |
1.01e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.97 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 429 GDPALLDLLNKAETlAGEESdPKLRLLGRHLKQLIDDgfNP----VVFCRYIATARYLHDHL------AGRF-------- 490
Cdd:COG1111 316 SDPRFRKAMRLAEE-ADIEH-PKLSKLREILKEQLGT--NPdsriIVFTQYRDTAEMIVEFLsepgikAGRFvgqaskeg 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 491 -RGVTVDvvtgefpaaERERRVDALGEAERRLLIATDCLSEGINLQEnLDAVVHYDLSWNPTRHEQREGRVDRFGQTSPK 569
Cdd:COG1111 392 dKGLTQK---------EQIEILERFRAGEFNVLVATSVAEEGLDIPE-VDLVIFYEPVPSEIRSIQRKGRTGRKREGRVV 461
|
170 180 190
....*....|....*....|....*....|...
gi 2792345535 570 VratLIygANNPVDGAVLQVILRKAEKIRQELG 602
Cdd:COG1111 462 V---LI--AKGTRDEAYYWSSRRKEKKMKSILK 489
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
120-377 |
9.54e-08 |
|
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: 54.61 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 120 LIADDVGIGKTIEA-ALIAReLQDRGEIQRMAIL--CPPHLVEQWVRElndrFHLHAVAVTATSAARLERGIPvGESLFQ 196
Cdd:pfam00176 21 ILADEMGLGKTLQTiSLLLY-LKHVDKNWGGPTLivVPLSLLHNWMNE----FERWVSPPALRVVVLHGNKRP-QERWKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 197 VH------PVTVVSLDYIkseRHRHDFIRAC-PEFVIVDEAHTcvsAGQGRQLRFELLRALaanEARHLVLLTATPHSGD 269
Cdd:pfam00176 95 DPnfladfDVVITTYETL---RKHKELLKKVhWHRIVLDEGHR---LKNSKSKLSKALKSL---KTRNRWILTGTPLQNN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 270 QDTFYSLLGLLKPE-FAALAT---------ASGDTKERLR--HQLALHFVQRRRPDIDEwqdGSIFPQREtaELTY-RLG 336
Cdd:pfam00176 166 LEELWALLNFLRPGpFGSLSTfrnwfdrpiERGGGKKGVSrlHKLLKPFLLRRTKKDVE---KSLPPKVE--YILFcRLS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2792345535 337 GLWENFFQDVLDYCR-EVVQRAGGDERSQRLSFWGTLALMRC 377
Cdd:pfam00176 241 KLQRKLYQTFLLKKDlNAIKTGEGGREIKASLLNILMRLRKI 282
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
119-264 |
2.62e-07 |
|
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: 50.86 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 119 LLIADDVGIGKTIEAALIARELQDRGEIQRMaILCPPH-LVEQWVRELNDRFHLHAVAVTATSAARLERGIPVGESLfqv 197
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL-VLVPTKaLALQTAERLRELFGPGIRVAVLVGGSSAEEREKNKLGD--- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792345535 198 HPVTVVSLDYI--KSERHRHDFIRACpEFVIVDEAHTCVSAGQGRQLRFELLRALAANEARhLVLLTAT 264
Cdd:cd00046 80 ADIIIATPDMLlnLLLREDRLFLKDL-KLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQ-VILLSAT 146
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
118-265 |
2.66e-07 |
|
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: 52.21 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 118 RLLIADDVGIGKTIEAALIARELQDRGEiqrMAILCPPHLVEQWVRELNdRFhLHAVAVTATSAARLER-GIPVGESLfq 196
Cdd:cd18010 18 RVLIADEMGLGKTVQAIAIAAYYREEWP---LLIVCPSSLRLTWADEIE-RW-LPSLPPDDIQVIVKSKdGLRDGDAK-- 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792345535 197 vhpVTVVSLDYikSERHRHDFIRACPEFVIVDEAHTCVSagqGRQLRFELLRALAAnEARHLVLLTATP 265
Cdd:cd18010 91 ---VVIVSYDL--LRRLEKQLLARKFKVVICDESHYLKN---SKAKRTKAALPLLK-RAKRVILLSGTP 150
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
120-282 |
7.04e-07 |
|
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: 51.20 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 120 LIADDVGIGKTIEAALIARELQDRGEIQRMAILCPPHLVEQWVRELNDRFHLHAVAVTATSAARL-----------ERGI 188
Cdd:cd18058 23 ILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYHGSQISRQmiqqyemyyrdEQGN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 189 PV-GESLFQvhpVTVVSLDYIKSErhrhdfiraCPEF-------VIVDEAHTCvsagqgRQLRFELLRALAANEARHLVL 260
Cdd:cd18058 103 PLsGIFKFQ---VVITTFEMILAD---------CPELkkinwscVIIDEAHRL------KNRNCKLLEGLKLMALEHKVL 164
|
170 180
....*....|....*....|..
gi 2792345535 261 LTATPHSGDQDTFYSLLGLLKP 282
Cdd:cd18058 165 LTGTPLQNSVEELFSLLNFLEP 186
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
119-267 |
1.29e-06 |
|
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: 49.16 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 119 LLIADDVGIGKTiEAALIA--RELQDRGEIQRMAILCPPH-LVEQWVRELNDRFHLHAVAVTATSAarlerGIPVGESLF 195
Cdd:pfam00270 17 VLVQAPTGSGKT-LAFLLPalEALDKLDNGPQALVLAPTReLAEQIYEELKKLGKGLGLKVASLLG-----GDSRKEQLE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792345535 196 QVHPVTVV-----SLDYIKSERHRHDFIRacpeFVIVDEAHTCVSAGQGRQLRfELLRALaaNEARHLVLLTATPHS 267
Cdd:pfam00270 91 KLKGPDILvgtpgRLLDLLQERKLLKNLK----LLVLDEAHRLLDMGFGPDLE-EILRRL--PKKRQILLLSATLPR 160
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
120-284 |
3.09e-06 |
|
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: 49.59 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 120 LIADDVGIGKTIEA-ALIARELQDRGEIQRMA-----------------ILCPPHLVEQWVRELND-------RFHLHAV 174
Cdd:cd18008 18 ILADEMGLGKTIQAlALILATRPQDPKIPEELeenssdpkklylskttlIVVPLSLLSQWKDEIEKhtkpgslKVYVYHG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 175 AVTATSAARLER--------GIPVGESLFQVHPVTVVSLDYIKSERHRHDFIRacpefVIVDEAHTCvsagqgRQLRFEL 246
Cdd:cd18008 98 SKRIKSIEELSDydivittyGTLASEFPKNKKGGGRDSKEKEASPLHRIRWYR-----VILDEAHNI------KNRSTKT 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 2792345535 247 LRALAANEARHLVLLTATPHSGDQDTFYSLLGLLKPEF 284
Cdd:cd18008 167 SRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEP 204
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
101-289 |
4.15e-06 |
|
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: 48.92 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 101 RTYQL--VPLLMALRLDPVRLLIADDVGIGKTIEA-ALIAReLQDRGEIQRMAILCPPHLVEQWVRELnDRF-------- 169
Cdd:cd18009 5 RPYQLegMEWLRMLWENGINGILADEMGLGKTIQTiALLAH-LRERGVWGPFLVIAPLSTLPNWVNEF-ARFtpsvpvll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 170 -HlhavaVTATSAARLERGIPVGESLFQVHPVTVVSLDYIKSERhrhDFIRACP-EFVIVDEAHTCvsagqgRQLRFELL 247
Cdd:cd18009 83 yH-----GTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDR---KALQHYAwKYLIVDEGHRL------KNLNCRLI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2792345535 248 RALAANEARHLVLLTATPHSGDQDTFYSLLGLLKPE-FAALAT 289
Cdd:cd18009 149 QELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDvFDDLSS 191
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
126-265 |
8.17e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 46.53 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 126 GIGKTIEAALIARELQdrgeIQRMAILCPP-HLVEQWVRELNDRFHLHAVAVTATSAARLERGIPVgeslfqvhPVTVVS 204
Cdd:cd17926 28 GSGKTLTALALIAYLK----ELRTLIVVPTdALLDQWKERFEDFLGDSSIGLIGGGKKKDFDDANV--------VVATYQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792345535 205 LDYIKSERHRhDFIRACpEFVIVDEAHTcVSAgqgrqlrfELLRALAANEARHLVL-LTATP 265
Cdd:cd17926 96 SLSNLAEEEK-DLFDQF-GLLIVDEAHH-LPA--------KTFSEILKELNAKYRLgLTATP 146
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
120-231 |
9.30e-06 |
|
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: 47.32 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 120 LIADDVGIGKTIEAALIARELQDRGEIQRMA-ILCPPHLVEQWVRELNDRFH------LHA---VAVTATSAARLERGIP 189
Cdd:cd18000 23 ILGDEMGLGKTIQIIAFLAALHHSKLGLGPSlIVCPATVLKQWVKEFHRWWPpfrvvvLHSsgsGTGSEEKLGSIERKSQ 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2792345535 190 VGESLFQVHPVTVVSLDYIKSerHRHDFIRACPEFVIVDEAH 231
Cdd:cd18000 103 LIRKVVGDGGILITTYEGFRK--HKDLLLNHNWQYVILDEGH 142
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
121-310 |
1.44e-05 |
|
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: 47.35 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 121 IADDVGIGKTIEA-ALIARELQDRGEIQRMA-----ILCPPHLVEQWVRELNDRFHLHAVAVTATSAARLERGIPVGEsl 194
Cdd:cd17999 24 LCDDMGLGKTLQTlCILASDHHKRANSFNSEnlpslVVCPPTLVGHWVAEIKKYFPNAFLKPLAYVGPPQERRRLREQ-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 195 FQVHPVTVVSLDYIKSErhrHDFIRACP-EFVIVDEAH------TCVSAGQgRQLRfellralaaneARHLVLLTATPHS 267
Cdd:cd17999 102 GEKHNVIVASYDVLRND---IEVLTKIEwNYCVLDEGHiiknskTKLSKAV-KQLK-----------ANHRLILSGTPIQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792345535 268 GDQDTFYSLLGLLKP-----------EFAALATASGDTK-------------ERLrHQLALHFVQRR 310
Cdd:cd17999 167 NNVLELWSLFDFLMPgylgtekqfqrRFLKPILASRDSKasakeqeagalalEAL-HKQVLPFLLRR 232
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
101-283 |
2.15e-05 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350817 [Multi-domain] Cd Length: 222 Bit Score: 46.56 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 101 RTYQL--VPLLMALRLDPVRLLIADDVGIGKTIEAALIARELQDRGEIQRMAILCPPHLVEQWVRELNDRFHLHAVAVTA 178
Cdd:cd18059 2 REYQLegVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 179 TSAARleRGIPVGESLFQVHPVTVvsldyIKSERHRHDFIRA-------CPEF-------VIVDEAHTCvsagqgRQLRF 244
Cdd:cd18059 82 SQASR--RTIQLYEMYFKDPQGRV-----IKGSYKFHAIITTfemiltdCPELrnipwrcVVIDEAHRL------KNRNC 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 2792345535 245 ELLRALAANEARHLVLLTATPHSGDQDTFYSLLGLLKPE 283
Cdd:cd18059 149 KLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPS 187
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
509-566 |
2.29e-05 |
|
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: 43.46 E-value: 2.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 509 RRVDALGEAERRL--LIATDCLSEGINLQeNLDAVVHYDLSWNPTRHEQREGRVDRFGQT 566
Cdd:cd18785 11 NSIEHAEEIASSLeiLVATNVLGEGIDVP-SLDTVIFFDPPSSAASYIQRVGRAGRGGKD 69
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
118-265 |
3.60e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 42.27 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 118 RLLIADDVGIGKTIEAALIARELQDRGEIQRMAILCP-PHLVEQWVRELNDRFHLHAVAVTATSAARLERGIPVGESLFq 196
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDDNKIVV- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792345535 197 vhpVTVVSLdYIKSERHRHDFIRACPEFVIVDEAHTcVSAGQGRQLrfellraLAANEARHLVLLTATP 265
Cdd:pfam04851 104 ---TTIQSL-YKALELASLELLPDFFDVIIIDEAHR-SGASSYRNI-------LEYFKPAFLLGLTATP 160
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
120-265 |
4.33e-04 |
|
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: 42.74 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 120 LIADDVGIGKTIEAALIARELQDRGEIQRMAILCPPHLVEQWVRELND--------RFHLHAVAVTATSAARLERGipvG 191
Cdd:cd18001 23 ILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKwtpglrvkVFHGTSKKERERNLERIQRG---G 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792345535 192 ESLFQVHPVTVVSLDYIKSERHRhdfiRACPEFVIVDEAHTCVSAGQGRQlrfELLRALAANearHLVLLTATP 265
Cdd:cd18001 100 GVLLTTYGMVLSNTEQLSADDHD----EFKWDYVILDEGHKIKNSKTKSA---KSLREIPAK---NRIILTGTP 163
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
491-565 |
5.23e-04 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 43.66 E-value: 5.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792345535 491 RGVTVDVVTGEFPAAERERRVDALGEAERRLLIATDCLSEGINLQEnLDAVVHYDLSWNPTRHEQREGRVDRFGQ 565
Cdd:PTZ00424 290 RDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQ-VSLVINYDLPASPENYIHRIGRSGRFGR 363
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
100-273 |
1.28e-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: 40.62 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 100 PRTYQLVPL--LMALRL-DPVRLLIADDVGIGKTIEAALIARELQDRGEIQRMAILCppH---LVEQWVRELNDRFHLHA 173
Cdd:cd18032 1 PRYYQQEAIeaLEEAREkGQRRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLA--HreeLLEQAERSFKEVLPDGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 174 VAvtatsaarlerGIPVGESLFQVHPVTVVSLDYIKSERHRHDFIRACPEFVIVDEAHTcVSAGQGRQLrfellraLAAN 253
Cdd:cd18032 79 FG-----------NLKGGKKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH-AIASSYRKI-------LEYF 139
|
170 180
....*....|....*....|.
gi 2792345535 254 EARHLVLLTATPHSGDQ-DTF 273
Cdd:cd18032 140 EPAFLLGLTATPERTDGlDTY 160
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
101-169 |
5.21e-03 |
|
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: 39.47 E-value: 5.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2792345535 101 RTYQLVPL--LMALRLDPVRLLIADDVGIGKTIEA-ALIARELQDRGEIQRMaILCPPHLVEQWVRELNdRF 169
Cdd:cd18012 6 RPYQKEGFnwLSFLRHYGLGGILADDMGLGKTLQTlALLLSRKEEGRKGPSL-VVAPTSLIYNWEEEAA-KF 75
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
448-559 |
5.34e-03 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 38.34 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792345535 448 SDPKLRLLGRHLK--QLIDDGFNPVVFCRYIATAR---YLHDHLAGRFRGVTVDVVTG-----EFPAAERERR-----VD 512
Cdd:cd18802 5 VIPKLQKLIEILReyFPKTPDFRGIIFVERRATAVvlsRLLKEHPSTLAFIRCGFLIGrgnssQRKRSLMTQRkqketLD 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2792345535 513 ALGEAERRLLIATDCLSEGINLQE-NLdaVVHYDLSWNPTRHEQREGR 559
Cdd:cd18802 85 KFRDGELNLLIATSVLEEGIDVPAcNL--VIRFDLPKTLRSYIQSRGR 130
|
|
| |
