|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
4-417 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 587.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlNGTPKALILVPTR 83
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR-PRAPQALILAPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 84 ELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMG 163
Cdd:COG0513 82 ELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 164 FWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVDKKRKRELLAYLIGSKNW 243
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 244 QQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFDMPFK 323
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 324 AEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQEWLAGFEPSLIEEVEPERHGGGGR-KSRSAEKRKL 402
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKlKGKKAGRGGR 401
|
410
....*....|....*
gi 520915635 403 KAKLAIHKNRGKNRR 417
Cdd:COG0513 402 PGPKGERKARRGKRR 416
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
3-416 |
4.78e-151 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 435.78 E-value: 4.78e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 3 VNFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTPK----ALI 78
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRrpvrALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 79 LVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADR 158
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 159 MLDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVDKKRKRELLAYLI 238
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 239 GSKNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINF 318
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 319 DMPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQEWLAGFEPSLIEEVEPERHGGGGRKSRSAE 398
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEPIQNGRQQRGGGGRG 400
|
410
....*....|....*...
gi 520915635 399 KRKLKAKLAIHKNRGKNR 416
Cdd:PRK10590 401 QGGGRGQQQGQPRRGEGG 418
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
5-393 |
2.57e-122 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 362.58 E-value: 2.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQsvqqeKLNGT---PKALILVP 81
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQ-----KLDVKrfrVQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 82 TRELAQQVFESLSQYASQTA-LRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRML 160
Cdd:PRK11776 81 TRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 161 DMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPnTTAETVTQIVYPVDKKRKRELLAYLIGS 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVEST-HDLPAIEQRFYEVSPDERLPALQRLLLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 241 KNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFDM 320
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520915635 321 PFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQEWLAGFEPSLIEEVEPERHG---GGGRK 393
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTlciDGGKK 395
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
4-417 |
7.01e-115 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 342.69 E-value: 7.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQ--EKLNGTPKALILVP 81
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDfpRRKSGPPRILILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 82 TRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLD 161
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 162 MGFWPDLQRILRRLPDEKQIMLFSATFE-KRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVD-KKRKRELLAYLIG 239
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADdLEHKTALLCHLLK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 240 SKNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFD 319
Cdd:PRK11192 242 QPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 320 MPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQEWLAGFEPSLIEEVEPERHGGGG-------- 391
Cdd:PRK11192 322 MPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAPSEKKTGKPSKkvlakrae 401
|
410 420
....*....|....*....|....*.
gi 520915635 392 RKSRSAEKRKLKAKLAIHKNRGKNRR 417
Cdd:PRK11192 402 KKEKEKEKPKVKKRHRDTKNIGKRRK 427
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
1-369 |
4.76e-102 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 311.46 E-value: 4.76e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 1 MSVNFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQ-----EKLNGTPK 75
Cdd:PRK01297 85 GKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQtpppkERYMGEPR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 76 ALILVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDG-ADILIATPGRLLDHLFNGNVNISKTNTLVLD 154
Cdd:PRK01297 165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 155 EADRMLDMGFWPDLQRILRRLP--DEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVDKKRKRE 232
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 233 LLAYLIGSKNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQEL 312
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 520915635 313 EQVINFDMPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQE 369
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCE 461
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-368 |
5.41e-102 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 316.02 E-value: 5.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 1 MSVNFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlnGTPKALILV 80
Cdd:PRK11634 4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPEL--KAPQILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 81 PTRELAQQVFESLSQYASQT-ALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRM 159
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 160 LDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVDKKRKRELLAYLIG 239
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 240 SKNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFD 319
Cdd:PRK11634 242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 520915635 320 MPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQ 368
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPE 370
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
5-417 |
2.14e-101 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 307.67 E-value: 2.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAF------GLPIIQSVQQEKLNGtPKALI 78
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFltatfhYLLSHPAPEDRKVNQ-PRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 79 LVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADR 158
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 159 MLDMGFWPDLQRILRRLPDEKQ--IMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQ-IVYPVDKKRKReLLA 235
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEeLFYPSNEEKMR-LLQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 236 YLIgSKNW-QQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQ 314
Cdd:PRK04837 248 TLI-EEEWpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 315 VINFDMPFKAEDYVHRIGRTGRAGNSGLAVSLMSrdEEYL--LHAIENLLDQRLPqewLAGFEPS-LIEEVEP----ERH 387
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLAC--EEYAlnLPAIETYIGHSIP---VSKYDSDaLLTDLPKplrlTRP 401
|
410 420 430
....*....|....*....|....*....|
gi 520915635 388 GGGGRKSRSAEKRklkaklaihkNRGKNRR 417
Cdd:PRK04837 402 RTGNGPRRSGAPR----------NRRRRKR 421
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
3-397 |
8.88e-101 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 310.17 E-value: 8.88e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 3 VNFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLP-IIQSVQQEKLN--GTPKALIL 79
Cdd:PTZ00110 130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPLLRygDGPIVLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 80 VPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRM 159
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 160 LDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLM-DSPVEIEVTPPN-TTAETVTQIVYPVDKKRKRELLAYL 237
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKML 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 238 IGS--KNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQV 315
Cdd:PTZ00110 370 LQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 316 INFDMPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLL---DQRLPQEwLAGFEPSLIEEVEPERHGGGGR 392
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLreaKQPVPPE-LEKLSNERSNGTERRRWGGYGR 528
|
....*
gi 520915635 393 KSRSA 397
Cdd:PTZ00110 529 FSNNV 533
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
14-207 |
1.55e-96 |
|
DEAD-box helicase domain of 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 287.03 E-value: 1.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSV--QQEKLNGTPKALILVPTRELAQQVFE 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 92 SLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQRI 171
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 520915635 172 LRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIE 207
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
3-369 |
1.16e-83 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 266.82 E-value: 1.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 3 VNFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQ-----EKLNGTPKAL 77
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSrpalaDRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 78 ILVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNV-NISKTNTLVLDEA 156
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 157 DRMLDMGFWPDLQRILRRLPDE--KQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVDKKRKRELL 234
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 235 AYLIGSKNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQ 314
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 520915635 315 VINFDMPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQE 369
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVE 383
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
5-201 |
3.86e-74 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350725 [Multi-domain] Cd Length: 221 Bit Score: 230.84 E-value: 3.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGT--------PKA 76
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgrgrrkayPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 77 LILVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEA 156
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520915635 157 DRMLDMGFWPDLQRILRR----LPDEKQIMLFSATFEKRIKTIAYKLMD 201
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLK 210
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
5-354 |
2.11e-73 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 238.53 E-value: 2.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGT-----PKALIL 79
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPseqrnPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 80 VPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRM 159
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 160 LDMGFWPDLQRILRRLPdEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVDKKRKRELLAYLIG 239
Cdd:PLN00206 283 LERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 240 SKNWQQ--VLVFTKTKQGSDELAKEL-KLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVI 316
Cdd:PLN00206 362 SKQHFKppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVI 441
|
330 340 350
....*....|....*....|....*....|....*...
gi 520915635 317 NFDMPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYL 354
Cdd:PLN00206 442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNL 479
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
5-360 |
3.49e-67 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 218.93 E-value: 3.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQeKLNGTpKALILVPTRE 84
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDY-DLNAC-QALILAPTRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 85 LAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGF 164
Cdd:PTZ00424 108 LAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 165 WPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPPNTTAETVTQIVYPVDKKR-KRELLAYLIGSKNW 243
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLYETLTI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 244 QQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFDMPFK 323
Cdd:PTZ00424 268 TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
|
330 340 350
....*....|....*....|....*....|....*..
gi 520915635 324 AEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLHAIEN 360
Cdd:PTZ00424 348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
5-207 |
2.13e-63 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 202.45 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQsvqqeKLNGTPK---ALILVP 81
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQ-----RLSEDPYgifALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 82 TRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNV---NISKTNTLVLDEADR 158
Cdd:cd17955 76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520915635 159 MLDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIE 207
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
14-206 |
2.14e-63 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 202.10 E-value: 2.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQ-QEKLNGTPKALILVPTRELAQQVFES 92
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLyRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 93 LSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNG-NVNISKTNTLVLDEADRMLDMGFWPDLQRI 171
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 520915635 172 LRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
27-195 |
2.19e-63 |
|
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: 200.93 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 27 TPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVqqEKLNGTPKALILVPTRELAQQVFESLSQYASQTALRIVC 106
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL--DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 107 VYGGISIGVQKKKLEdGADILIATPGRLLDHLFNgNVNISKTNTLVLDEADRMLDMGFWPDLQRILRRLPDEKQIMLFSA 186
Cdd:pfam00270 79 LLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
....*....
gi 520915635 187 TFEKRIKTI 195
Cdd:pfam00270 157 TLPRNLEDL 165
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-200 |
2.28e-63 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 204.43 E-value: 2.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGT-------PKA 76
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASsfsevqePQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 77 LILVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEA 156
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 520915635 157 DRMLDMGFWPDLQRILRRL--PD--EKQIMLFSATFEKRIKTIAYKLM 200
Cdd:cd18052 204 DRMLDMGFGPEIRKLVSEPgmPSkeDRQTLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
5-207 |
6.05e-63 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 201.39 E-value: 6.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVqqekLNGTPK--ALILVPT 82
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL----LENPQRffALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 83 RELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGN-VNISKTNTLVLDEADRMLD 161
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520915635 162 MGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIE 207
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
218-346 |
1.75e-59 |
|
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: 189.64 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 218 VTQIVYPVDKKRKRE-LLAYLIGSKNWQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRA 296
Cdd:cd18787 1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 520915635 297 LIATDVAARGLDIQELEQVINFDMPFKAEDYVHRIGRTGRAGNSGLAVSL 346
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITF 130
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
13-202 |
1.54e-58 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 190.10 E-value: 1.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 13 NLVETLSTLNIVTPTPVQEKSIPHVLE-GKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTP---KALILVPTRELAQQ 88
Cdd:cd17964 4 SLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRsgvSALIISPTRELALQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 89 VFE---SLSQYasQTALRIVCVYGGISIGVQKKKLE-DGADILIATPGRLLDHLFNGNVNI--SKTNTLVLDEADRMLDM 162
Cdd:cd17964 84 IAAeakKLLQG--LRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAKafTDLDYLVLDEADRLLDM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 520915635 163 GFWPDLQRILRRLP----DEKQIMLFSATFEKRIKTIAYKLMDS 202
Cdd:cd17964 162 GFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
4-206 |
5.23e-58 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 189.13 E-value: 5.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQ-QEKLNGT--PKALILV 80
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdQRPVKPGegPIGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 81 PTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLF--NGNV-NISKTNTLVLDEAD 157
Cdd:cd17953 93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTanNGRVtNLRRVTYVVLDEAD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520915635 158 RMLDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17953 173 RMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
14-206 |
2.05e-56 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 184.11 E-value: 2.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQ--SVQQEKLNGT-PKALILVPTRELAQQVF 90
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVhiNAQPPLERGDgPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 91 ESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQR 170
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 520915635 171 ILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
14-206 |
3.47e-56 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 183.77 E-value: 3.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSV--QQEKLNGT-PKALILVPTRELAQQVF 90
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKGEgPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 91 ESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQR 170
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 520915635 171 ILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
14-206 |
3.90e-56 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 184.45 E-value: 3.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQ------EKLNGTPKALILVPTRELAQ 87
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppldeETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 88 QVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPD 167
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 520915635 168 LQRILRRLPDE--------------------KQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17945 161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
18-221 |
4.33e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 183.46 E-value: 4.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 18 LSTLNIVTPTPVQEKSIPHVLEG-KNLLAAAQTGTGKTAAFGLPIIQSVQQEKlngTPKALILVPTRELAQQVFESLSQY 96
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 97 ASQTALRIVCVYGGISIGVQKKKLEDG-ADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQRILRRL 175
Cdd:smart00487 78 GPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520915635 176 PDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEVTPpnTTAETVTQI 221
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
4-201 |
2.73e-55 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 183.32 E-value: 2.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPII---------QSVQQEKLNGT- 73
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsqiyeqgpgESLPSESGYYGr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 74 ----PKALILVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTN 149
Cdd:cd18051 102 rkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 520915635 150 TLVLDEADRMLDMGFWPDLQRILRR--LP--DEKQIMLFSATFEKRIKTIAYKLMD 201
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEQdtMPptGERQTLMFSATFPKEIQMLARDFLD 237
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
5-206 |
1.67e-54 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 179.42 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNgtPKALILVPTRE 84
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV--IQALILVPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 85 LAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGF 164
Cdd:cd17940 79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 520915635 165 WPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17940 159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
10-204 |
5.13e-53 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 175.85 E-value: 5.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 10 IEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGT----PKALILVPTREL 85
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGeeqgTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 86 AQQV---FESLSQYASQtALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGN-VNISKTNTLVLDEADRMLD 161
Cdd:cd17961 81 AQQVskvLEQLTAYCRK-DVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSlLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520915635 162 MGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPV 204
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
4-190 |
5.91e-53 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 175.57 E-value: 5.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTPKALILVPTR 83
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 84 ELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMG 163
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180
....*....|....*....|....*..
gi 520915635 164 FWPDLQRILRRLPDEKQIMLFSATFEK 190
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPK 188
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
3-208 |
1.04e-52 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 175.97 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 3 VNFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQ----EKLNGtPKALI 78
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHqpflERGDG-PICLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 79 LVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADR 158
Cdd:cd18049 103 LAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520915635 159 MLDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEV 208
Cdd:cd18049 183 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
14-187 |
2.83e-52 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 173.53 E-value: 2.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTPK---ALILVPTRELAQQVF 90
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGqvgALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 91 ESLSQYAS--QTALRIVCVYGGISIGVQKKKL-EDGADILIATPGRLLDhLFNGNVNISKTNT---LVLDEADRMLDMGF 164
Cdd:cd17960 81 EVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEE-LLSRKADKVKVKSlevLVLDEADRLLDLGF 159
|
170 180
....*....|....*....|...
gi 520915635 165 WPDLQRILRRLPDEKQIMLFSAT 187
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSAT 182
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
24-208 |
9.24e-52 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 172.09 E-value: 9.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 24 VTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTPK--ALILVPTRELAQQVFESLSQYASQTA 101
Cdd:cd17941 11 IKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGlgALIISPTRELAMQIFEVLRKVGKYHS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 102 LRIVCVYGGISIGVQKKKLeDGADILIATPGRLLDHLfNGNVNISKTN--TLVLDEADRMLDMGFWPDLQRILRRLPDEK 179
Cdd:cd17941 91 FSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHM-DETPGFDTSNlqMLVLDEADRILDMGFKETLDAIVENLPKSR 168
|
170 180
....*....|....*....|....*....
gi 520915635 180 QIMLFSATFEKRIKTIAYKLMDSPVEIEV 208
Cdd:cd17941 169 QTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
14-208 |
2.26e-49 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 165.84 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTPKALILVPTRELAQQVFESL 93
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 94 SQYASQTALRIVCVYGGiSIGVQKKKLEDG--ADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQRI 171
Cdd:cd17957 81 LKLSKGTGLRIVLLSKS-LEAKAKDGPKSItkYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 520915635 172 LRRLPD-EKQIMLFSATFEKRIKTIAYKLMDSPVEIEV 208
Cdd:cd17957 160 LAACTNpNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
5-204 |
5.56e-49 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 165.19 E-value: 5.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQqeklngtpkALILVPTRE 84
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV---------ALILEPSRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 85 LAQQV---FESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLD 161
Cdd:cd17938 72 LAEQTyncIENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 520915635 162 MGFWPDLQRILRRLP----DEK--QIMLFSAT---FEkrIKTIAYKLMDSPV 204
Cdd:cd17938 152 QGNLETINRIYNRIPkitsDGKrlQVIVCSATlhsFE--VKKLADKIMHFPT 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
14-188 |
1.19e-48 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 165.49 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPH-VLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEK-------LNGTPKALILVPTREL 85
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKssngvggKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 86 AQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGN---VNISKTNTLVLDEADRMLDM 162
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 520915635 163 GFWPDLQRILRRLPDE-------KQIMLFSATF 188
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL 193
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
14-206 |
1.88e-48 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 163.79 E-value: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLP-----IIQSVQQEKLNGtPKALILVPTRELAQQ 88
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihlDLQPIPREQRNG-PGVLVLTPTRELALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 89 VFESLSQYaSQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDL 168
Cdd:cd17958 80 IEAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 520915635 169 QRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
4-208 |
3.82e-48 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 165.18 E-value: 3.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQ----EKLNGtPKALIL 79
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHqpylERGDG-PICLVL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 80 VPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRM 159
Cdd:cd18050 142 APTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520915635 160 LDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEV 208
Cdd:cd18050 222 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
27-196 |
9.22e-48 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 161.76 E-value: 9.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 27 TPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQ---SVQQEKLNGTpKALILVPTRELAQQVF---ESLSQYASQT 100
Cdd:cd17942 14 TEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLKFKPRNGT-GVIIISPTRELALQIYgvaKELLKYHSQT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 101 ALrivCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKT-NTLVLDEADRMLDMGFWPDLQRILRRLPDEK 179
Cdd:cd17942 93 FG---IVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNlQCLIIDEADRILEIGFEEEMRQIIKLLPKRR 169
|
170
....*....|....*..
gi 520915635 180 QIMLFSATFEKRIKTIA 196
Cdd:cd17942 170 QTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
14-206 |
4.41e-47 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 160.44 E-value: 4.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLST-LNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQ--QEKLNGT--PKALILVPTRELAQQ 88
Cdd:cd17949 1 LVSHLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLslEPRVDRSdgTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 89 VFESLsqyasQTALR----IVCvygGISIGVQKKK-----LEDGADILIATPGRLLDHLFNGNV-NISKTNTLVLDEADR 158
Cdd:cd17949 81 IYEVL-----EKLLKpfhwIVP---GYLIGGEKRKsekarLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520915635 159 MLDMGFWPDLQRILRRLPDE-------------KQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17949 153 LLDMGFEKDITKILELLDDKrskaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-208 |
4.67e-46 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 157.89 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 2 SVNFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQsvQQEKLNGTPKALILVP 81
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQ--QLEPVDGQVSVLVICH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 82 TRELAQQV---FESLSQYASQTalRIVCVYGGISIGVQKKKLEDGA-DILIATPGRLLDHLFNGNVNISKTNTLVLDEAD 157
Cdd:cd17950 79 TRELAFQIsneYERFSKYMPNV--KTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 520915635 158 RM---LDMGfwPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIEV 208
Cdd:cd17950 157 KMleqLDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
14-206 |
1.95e-44 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 153.26 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPII-QSVQQEKL-----NGTPKALILVPTRELAQ 87
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImFALEQEKKlpfikGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 88 QVFESLSQY------ASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLD 161
Cdd:cd17951 81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520915635 162 MGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
7-206 |
4.52e-44 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 152.09 E-value: 4.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 7 DLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlnGTPKALILVPTRELA 86
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV--RETQALVLAPTRELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 87 QQ---VFESLSQYASQTALriVCVyGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMG 163
Cdd:cd17939 79 QQiqkVVKALGDYMGVKVH--ACI-GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520915635 164 FWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
13-206 |
8.37e-43 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 148.88 E-value: 8.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 13 NLVETLSTLNIVTPTPVQEKSIPHVLEG--KNLLAAAQTGTGKTAAFGLPIIQSVQQEklNGTPKALILVPTRELAQQVF 90
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPT--LKSPQALCLAPTRELARQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 91 ESLSQYASQTALRIVCVYGGISIGVQKKKledGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDM-GFWPDLQ 169
Cdd:cd17963 82 EVVEKMGKFTGVKVALAVPGNDVPRGKKI---TAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 520915635 170 RILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17963 159 RIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
28-205 |
9.03e-42 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, 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. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 146.15 E-value: 9.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 28 PVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPII---QSVQQEKLNG-TPKALILVPTRELAQQVFESLSQYASQtaLR 103
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIeklQEDQQPRKRGrAPKVLVLAPTRELANQVTKDFKDITRK--LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 104 IVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQRILRRL-----PDE 178
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDN 172
|
170 180
....*....|....*....|....*..
gi 520915635 179 KQIMLFSATFEKRIKTIAYKLMDSPVE 205
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
26-206 |
1.26e-39 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 140.38 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 26 PTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNgtPKALILVPTRELAQQVFESLSQYASQTA-LRI 104
Cdd:cd17962 13 PTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN--PSALILTPTRELAVQIEDQAKELMKGLPpMKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 105 VCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQRILRRLPDEKQIMLF 184
Cdd:cd17962 91 ALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTILV 170
|
170 180
....*....|....*....|..
gi 520915635 185 SATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd17962 171 SATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
14-211 |
7.23e-39 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 139.42 E-value: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLN-----GTPKALILVPTRELAQQ 88
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaegpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 89 ---VFESLSQYasqTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFW 165
Cdd:cd17948 81 igsVAQSLTEG---LGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 520915635 166 PDLQRILRRLP--------DEK-----QIMLFSATFEKRIKTIAYKLMDSPVEIEVTPP 211
Cdd:cd17948 158 EKLSHFLRRFPlasrrsenTDGldpgtQLVLVSATMPSGVGEVLSKVIDVDSIETVTSD 216
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
14-207 |
5.61e-37 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 133.16 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEklNGTPKALILVPTRELA---QQVF 90
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE--RRHPQVLILAPTREIAvqiHDVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 91 ESLSQYAsqTALRiVCVY-GGISIGVQKKKLEdGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQ 169
Cdd:cd17943 79 KKIGKKL--EGLK-CEVFiGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 520915635 170 RILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEIE 207
Cdd:cd17943 155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
5-206 |
1.48e-36 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 132.57 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEkLNGTpKALILVPTRE 84
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS-LKAT-QALVLAPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 85 LAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGF 164
Cdd:cd18046 79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 520915635 165 WPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd18046 159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
14-187 |
3.51e-36 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 132.37 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 14 LVETLSTLNIVTPTPVQEKSIPHVLEG---------KNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTpKALILVPTRE 84
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRL-RALIVVPTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 85 LAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKL--------EDGADILIATPGRLLDHLfNGNVNIS--KTNTLVLD 154
Cdd:cd17956 80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLlvdtsgryLSRVDILVATPGRLVDHL-NSTPGFTlkHLRFLVID 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 520915635 155 EADRMLDMGF--WPD-LQRILRRLPDEK-----------------QIMLFSAT 187
Cdd:cd17956 159 EADRLLNQSFqdWLEtVMKALGRPTAPDlgsfgdanllersvrplQKLLFSAT 211
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
5-206 |
1.37e-33 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 124.50 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVqqEKLNGTPKALILVPTRE 84
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQVRETQALILSPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 85 LAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGF 164
Cdd:cd18045 79 LAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 520915635 165 WPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSPVEI 206
Cdd:cd18045 159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
230-338 |
9.71e-33 |
|
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: 119.24 E-value: 9.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 230 KRELLAYLIGSKNWQQVLVFTKTKQGSDElAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDI 309
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 520915635 310 QELEQVINFDMPFKAEDYVHRIGRTGRAG 338
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
10-212 |
1.18e-29 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 115.55 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 10 IEQNLVETLSTLNIVTPTPVQEKSIPHVLEG----------------KNLLAAAQTGTGKTAAFGLPII----------- 62
Cdd:cd17965 15 IKEILKGSNKTDEEIKPSPIQTLAIKKLLKTlmrkvtkqtsneepklEVFLLAAETGSGKTLAYLAPLLdylkrqeqepf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 63 ----QSVQQEKLNGTPKALILVPTRELAQQVFESLSQYASQTALRIVCVYGGISIGVQKKKL--EDGADILIATPGRLLD 136
Cdd:cd17965 95 eeaeEEYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLafKGRIDILVTTPGKLAS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520915635 137 hLFNGNVNI-SKTNTLVLDEADRMLDMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMdsPVEIEVTPPN 212
Cdd:cd17965 175 -LAKSRPKIlSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLF--PDVVRIATPR 248
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
4-203 |
1.61e-27 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 108.96 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 4 NFADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEG--KNLLAAAQTGTGKTAAFGLPIIQSVQQEKLngTPKALILVP 81
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKL--YPQCLCLSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 82 TRELAQQ---VFESLSQYASqtALRIVCVYGGISIGvQKKKLEdgADILIATPGRLLDHLFNGN-VNISKTNTLVLDEAD 157
Cdd:cd18048 97 TFELALQtgkVVEEMGKFCV--GIQVIYAIRGNRPG-KGTDIE--AQIVIGTPGTVLDWCFKLRlIDVTNISVFVLDEAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520915635 158 RMLDM-GFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSP 203
Cdd:cd18048 172 VMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
257-338 |
2.00e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 103.83 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 257 DELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFDMPFKAEDYVHRIGRTGR 336
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 520915635 337 AG 338
Cdd:smart00490 81 AG 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
5-364 |
9.66e-24 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 103.76 E-value: 9.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADL--GIEQNLVETLSTLNIVTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQeklNGTPKALILVPT 82
Cdd:COG1205 34 YAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE---DPGATALYLYPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 83 RELAQ-QVfESLSQYASQTALRI-VCVYGGISIGVQKKKLEDGADILIATP-----GRLLDH-----LFngnvniSKTNT 150
Cdd:COG1205 111 KALARdQL-RRLRELAEALGLGVrVATYDGDTPPEERRWIREHPDIVLTNPdmlhyGLLPHHtrwarFF------RNLRY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 151 LVLDEA---------------DRmldmgfwpdLQRILRRLPDEKQIMLFSAT-------FEKRI---------------- 192
Cdd:COG1205 184 VVIDEAhtyrgvfgshvanvlRR---------LRRICRHYGSDPQFILASATignpaehAERLTgrpvtvvdedgsprge 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 193 KTIAykLMDSPVEIEVTPPNTTAETvtqivypvdkkrkRELLAYLIGSKnwQQVLVFTKTKQGSDELAKELK---LDGIK 269
Cdd:COG1205 255 RTFV--LWNPPLVDDGIRRSALAEA-------------ARLLADLVREG--LRTLVFTRSRRGAELLARYARralREPDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 270 AVSI---NGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFDMPFKAEDYVHRIGRTGRAGNSGLAVSL 346
Cdd:COG1205 318 ADRVaayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV 397
|
410 420
....*....|....*....|
gi 520915635 347 MSRD--EEYLLHAIENLLDQ 364
Cdd:COG1205 398 AGDDplDQYYVRHPEELFER 417
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
40-187 |
4.17e-23 |
|
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: 94.39 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 40 GKNLLAAAQTGTGKTAAFGLPIIQSVqqekLNGTPKALILVPTRELAQQVFESLSQYASQtALRIVCVYGGISIGVQKKK 119
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL----LKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520915635 120 LEDGADILIATPGRLL-DHLFNGNVNISKTNTLVLDEADRMLDMGF--WPDLQRILRRLPDEKQIMLFSAT 187
Cdd:cd00046 76 KLGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRgaLILDLAVRKAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
40-386 |
1.26e-22 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 100.10 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 40 GKNLLAAAqTGTGKT--AAFglpIIQSVQQEKlngtpKALILVPTRELAQQVFESLSQyasqtalrivcVYGGISIGVQK 117
Cdd:COG1061 101 GRGLVVAP-TGTGKTvlALA---LAAELLRGK-----RVLVLVPRRELLEQWAEELRR-----------FLGDPLAGGGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 118 KklEDGADILIATP----GRLLDHLFNGNVNIsktntLVLDEADRMLDMGFwpdlQRILRRLPDeKQIMLFSAT------ 187
Cdd:COG1061 161 K--DSDAPITVATYqslaRRAHLDELGDRFGL-----VIIDEAHHAGAPSY----RRILEAFPA-AYRLGLTATpfrsdg 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 188 -------FEKRIKTIAYK-LMDS---------PVEIEVTPPNTTAETVTQIVYPV---DKKRKRELL-AYLIGSKNWQQV 246
Cdd:COG1061 229 reillflFDGIVYEYSLKeAIEDgylappeyyGIRVDLTDERAEYDALSERLREAlaaDAERKDKILrELLREHPDDRKT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 247 LVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVInFDMPFKAE- 325
Cdd:COG1061 309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPr 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520915635 326 DYVHRIGR---TGRAGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQEWLAGFEPSLIEEVEPER 386
Cdd:COG1061 388 EFIQRLGRglrPAPGKEDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAV 451
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
5-203 |
8.27e-19 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 84.39 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 5 FADLGIEQNLVETLSTLNIVTPTPVQEKSIPHVLEG--KNLLAAAQTGTGKTAAFGLPIIQSVqqEKLNGTPKALILVPT 82
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 83 RELAQQ---VFESLSQYASQTALrivcvyggiSIGVQKKKLEDGA----DILIATPGRLLDHLFNGN-VNISKTNTLVLD 154
Cdd:cd18047 81 YELALQtgkVIEQMGKFYPELKL---------AYAVRGNKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520915635 155 EADRML-DMGFWPDLQRILRRLPDEKQIMLFSATFEKRIKTIAYKLMDSP 203
Cdd:cd18047 152 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-338 |
8.87e-19 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 88.41 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 1 MSVnfADLGIEqNLVETLSTLNIVTPTPVQEKSIP-HVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlngtpKALIL 79
Cdd:COG1204 1 MKV--AELPLE-KVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG-----KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 80 VPTRELAQQVFESLSQYASQTALRIVCVYGGISIGvqKKKLEDgADILIATPGRlLDHLF-NGNVNISKTNTLVLDEAdR 158
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEK-LDSLLrNGPSWLRDVDLVVVDEA-H 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 159 ML-DMGFWPDLQRI---LRRLPDEKQIMLFSATFEKrIKTIAyKLMD-SPVEIEVTPPNTTAETVTQ-IVYPVDKKR--K 230
Cdd:COG1204 148 LIdDESRGPTLEVLlarLRRLNPEAQIVALSATIGN-AEEIA-EWLDaELVKSDWRPVPLNEGVLYDgVLRFDDGSRrsK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 231 RELLAYLIGS-KNWQQVLVFTKTKQGSDELAKEL---------------------KLDGIKAVSINGDK----------- 277
Cdd:COG1204 226 DPTLALALDLlEEGGQVLVFVSSRRDAESLAKKLadelkrrltpeereeleelaeELLEVSEETHTNEKladclekgvaf 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520915635 278 -----SQGARQRALDEFKQGKVRALIATD-------VAARGLDIQELEQviNFDMPFKAEDYVHRIGRTGRAG 338
Cdd:COG1204 306 hhaglPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKR--GGMVPIPVLEFKQMAGRAGRPG 376
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
231-353 |
5.40e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 80.16 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 231 RELLAYLIGSKNWQQVLVFTKTKQGSDELAKELKLDGIKAV------SINGDK--SQGARQRALDEFKQGKVRALIATDV 302
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 520915635 303 AARGLDIQELEQVINFDmPFKAE-DYVHRIGRTGRaGNSGLAVSLM---SRDEEY 353
Cdd:COG1111 421 AEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGR-KREGRVVVLIakgTRDEAY 473
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-187 |
1.28e-14 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 71.52 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 25 TPTPVQEKSIPHV-LEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlngtPKALILVPTRELAQQVFESLSQYASQTALR 103
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSG----GKAVYIAPTRALVNQKEADLRERFGPLGKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 104 IVCVYGGISIgvqKKKLEDGADILIATPGRLLDHLFNG-NVNISKTNTLVLDEADRMLDMGFWPDLQRILRRLPDEK--- 179
Cdd:cd17921 77 VGLLTGDPSV---NKLLLAEADILVATPEKLDLLLRNGgERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINkna 153
|
....*...
gi 520915635 180 QIMLFSAT 187
Cdd:cd17921 154 RFVGLSAT 161
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
231-353 |
4.38e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 71.06 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 231 RELLAYLIGSKNWQQVLVFTKTKQGSDELAKELKLDGIKAV------SINGDK--SQGARQRALDEFKQGKVRALIATDV 302
Cdd:PRK13766 353 REIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVrfvgqaSKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSV 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 520915635 303 AARGLDIQELEQVInFDMPFKAE-DYVHRIGRTGRaGNSGLAVSLMS---RDEEY 353
Cdd:PRK13766 433 AEEGLDIPSVDLVI-FYEPVPSEiRSIQRKGRTGR-QEEGRVVVLIAkgtRDEAY 485
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
28-369 |
1.14e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 69.40 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 28 PVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLP--------IIQS---------VQQEKLNGTPKALI---LvpTRELAQ 87
Cdd:COG0514 20 PGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalllpgltLVVSplialmkdqVDALRAAGIRAAFLnssL--SAEERR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 88 QVFEslsqyasqtalrivcvyggisigvqkkKLEDGA-DILIATPGRL-----LDHLfnGNVNISktnTLVLDEA----- 156
Cdd:COG0514 98 EVLR---------------------------ALRAGElKLLYVAPERLlnprfLELL--RRLKIS---LFAIDEAhcisq 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 157 ---DrmldmgFWPD---LQRILRRLPDeKQIMLFSATFEKR-IKTIAYKL-MDSPVEIeVTP---PNTTaetvTQIVYPV 225
Cdd:COG0514 146 wghD------FRPDyrrLGELRERLPN-VPVLALTATATPRvRADIAEQLgLEDPRVF-VGSfdrPNLR----LEVVPKP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 226 DKKRKRELLAYLIGSKNwQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIATdVA-A 304
Cdd:COG0514 214 PDDKLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfG 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520915635 305 RGLDIQELEQVINFDMPFKAEDYVHRIGRTGRAGNSGLAVSLMSRDEEYLLhaiENLLDQRLPQE 369
Cdd:COG0514 292 MGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQ---RFFIEQSPPDE 353
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
231-332 |
1.49e-12 |
|
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: 64.42 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 231 RELLAYLIGSKnwQQVLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGK--VRALIATDVAARGLD 308
Cdd:cd18793 17 LELLEELREPG--EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLN 94
|
90 100 110
....*....|....*....|....*....|
gi 520915635 309 IQELEQVINFDMPFK------AEDYVHRIG 332
Cdd:cd18793 95 LTAANRVILYDPWWNpaveeqAIDRAHRIG 124
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
30-187 |
2.78e-12 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 64.91 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 30 QEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlngTPKALILVPTRELAQQVFESLSQYASQTALRIVC-VY 108
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP---GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVaTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 109 GG-ISIGVQKKKLEDGADILIATPgRLLDH--LFNGNVNISKTNTL---VLDEAdRMLDMGFWPD-------LQRILRRL 175
Cdd:cd17923 82 DGdTPREERRAIIRNPPRILLTNP-DMLHYalLPHHDRWARFLRNLryvVLDEA-HTYRGVFGSHvalllrrLRRLCRRY 159
|
170
....*....|..
gi 520915635 176 PDEKQIMLFSAT 187
Cdd:cd17923 160 GADPQFILTSAT 171
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
24-156 |
1.46e-10 |
|
DEXH-box helicase domain of 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. Dicers exist throughout eukaryotes, and a subset have 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 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 60.36 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 24 VTPTPVQEKSIPHVLEgKNLLAAAQTGTGKT--AAFGLPIIQSVQQEKLNGTPKALILVPTRELAQQVFESLSQYasqTA 101
Cdd:cd18034 1 FTPRSYQLELFEAALK-RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSH---TD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 520915635 102 LRIVCVYG--GISIGVQKKKLE--DGADILIATPGRLLDHLFNGNVNISKTNTLVLDEA 156
Cdd:cd18034 77 LKVGEYSGemGVDKWTKERWKEelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
24-158 |
8.45e-10 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 58.21 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 24 VTPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTPKALILVPTRELAQQVFESLSQYASQTALR 103
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 520915635 104 IVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGN-VNISKTNTLVLDEADR 158
Cdd:cd17927 81 VTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTiVSLSDFSLLVFDECHN 136
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
28-187 |
1.26e-09 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 56.96 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 28 PVQEKSIPH-VLEGKNLLAAAQTGTGKTAAFGLPIIQSVqqekLNGTpKALILVPTRELAQQVFESLSQYaSQTALRIvc 106
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTL----LEGG-KALYLVPLRALASEKYEEFKKL-EEIGLKV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 107 vygGISIGVQKKKLE--DGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQRI---LRRLPDEKQI 181
Cdd:cd18028 76 ---GISTGDYDEDDEwlGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIvarLRRLNPNTQI 152
|
....*.
gi 520915635 182 MLFSAT 187
Cdd:cd18028 153 IGLSAT 158
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
222-338 |
2.45e-09 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 55.29 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 222 VYPVDKKRKRELLAYLIGSKNWQQ-VLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGKVRALIAT 300
Cdd:cd18794 8 VRPKDKKDEKLDLLKRIKVEHLGGsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 520915635 301 dVA-ARGLDIQELEQVINFDMPFKAEDYVHRIGRTGRAG 338
Cdd:cd18794 88 -VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
244-347 |
2.67e-09 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 55.44 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 244 QQVLVFTKTKQGSDELAKELK--LDGIKAVSI----NGDKSQGARQR----ALDEFKQGKVRALIATDVAARGLDIQELE 313
Cdd:cd18801 31 TRVIIFSEFRDSAEEIVNFLSkiRPGIRATRFigqaSGKSSKGMSQKeqkeVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
|
90 100 110
....*....|....*....|....*....|....
gi 520915635 314 QVINFDMPFKAEDYVHRIGRTGRaGNSGLAVSLM 347
Cdd:cd18801 111 LIICYDASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
247-340 |
4.03e-09 |
|
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: 54.90 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 247 LVFTKTKQGSDELAK-----ELKLDGIKA------VSINGDKSQGARQR----ALDEFKQGKVRALIATDVAARGLDIQE 311
Cdd:cd18802 29 IIFVERRATAVVLSRllkehPSTLAFIRCgfligrGNSSQRKRSLMTQRkqkeTLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100
....*....|....*....|....*....
gi 520915635 312 LEQVINFDMPFKAEDYVHRIGRtGRAGNS 340
Cdd:cd18802 109 CNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
246-334 |
6.66e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 57.93 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 246 VLVFTKTKQGSDELAKELKLDGIKAVSINGDKSQGARQRALDEFKQGK--VRALIATDVAARGLDIQELEQVINFDMPF- 322
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWn 631
|
90
....*....|....*..
gi 520915635 323 -----KAEDYVHRIGRT 334
Cdd:COG0553 632 paveeQAIDRAHRIGQT 648
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
243-341 |
2.94e-08 |
|
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: 50.40 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 243 WQQVLVFTKTKQGSDELAKELKLdgikavsingdksqgarqraldefkqgkvraLIATDVAARGLDIQELEQVINFDMPF 322
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLEI-------------------------------LVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90
....*....|....*....
gi 520915635 323 KAEDYVHRIGRTGRAGNSG 341
Cdd:cd18785 52 SAASYIQRVGRAGRGGKDE 70
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
28-319 |
7.38e-08 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 54.51 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 28 PVQEKSIPH-VLEGKNLLAAAQTGTGKTAAFGLPIIQSVqqekLNGTPKALILVPTRELAQQVFESLS-QYAS--QTALR 103
Cdd:COG1202 212 PVQSLAVENgLLEGKDQLVVSATATGKTLIGELAGIKNA----LEGKGKMLFLVPLVALANQKYEDFKdRYGDglDVSIR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 104 IvcvyGGISIGVQKKKLEDGADILIAT-PGrlLDHLFNGNVNISKTNTLVLDEAdRMLDmgfwpDLQR-------I--LR 173
Cdd:COG1202 288 V----GASRIRDDGTRFDPNADIIVGTyEG--IDHALRTGRDLGDIGTVVIDEV-HMLE-----DPERghrldglIarLK 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 174 RLPDEKQIMLFSATFEKRiKTIAYKLMDSPVEIEVTPpnttaetVT---QIVYpVDKKRKRELLAYL-------IGSKNW 243
Cdd:COG1202 356 YYCPGAQWIYLSATVGNP-EELAKKLGAKLVEYEERP-------VPlerHLTF-ADGREKIRIINKLvkrefdtKSSKGY 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520915635 244 Q-QVLVFTKTKQGSDELAKELkldGIKAVSINGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQElEQVInFD 319
Cdd:COG1202 427 RgQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPA-SQVI-FD 498
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
25-131 |
1.14e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 53.95 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 25 TPTPVQEKSIPHVLEGKNLLAAAQTGTGKT-AAFgLPII-----QSVQQEKLNG------TP-KAL-------ILVPTRE 84
Cdd:COG1201 24 APTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALdelarRPRPGELPDGlrvlyiSPlKALandiernLRAPLEE 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 520915635 85 LAQQVFESLSqyasqtalrivcvygGISIGV------------QKKKLedgADILIATP 131
Cdd:COG1201 103 IGEAAGLPLP---------------EIRVGVrtgdtpaserqrQRRRP---PHILITTP 143
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
229-341 |
1.51e-07 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 50.71 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 229 RKRELLAYLIGS-KNWQQVLVFTKTKQGSDELAKELKLDGIkavsiNGDKSQGARQRALDEFKQGKVRALIATDVAARGL 307
Cdd:cd18789 34 NKLRALEELLKRhEQGDKIIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
|
90 100 110
....*....|....*....|....*....|....*
gi 520915635 308 DIQELEQVINFDMPFKAE-DYVHRIGRTGRAGNSG 341
Cdd:cd18789 109 DLPEANVAIQISGHGGSRrQEAQRLGRILRPKKGG 143
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
29-158 |
3.45e-07 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 50.21 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 29 VQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlngtPKALILVPTRELAQQVFESLSQYASqTALRIVCVY 108
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKG----GKVLILAPSRPLVEQHAENLKRVLN-IPDKITSLT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 520915635 109 GGISIGvQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADR 158
Cdd:cd18035 80 GEVKPE-ERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
40-155 |
3.74e-07 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 49.50 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 40 GKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTpKALILVPTRELAQQVFESLSQYASQTAL--RIVCVYGGISIGVQK 117
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV-QVLYISPLKALINDQERRLEEPLDEIDLeiPVAVRHGDTSQSEKA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 520915635 118 KKLEDGADILIATPGRL--------LDHLFNGnvniskTNTLVLDE 155
Cdd:cd17922 80 KQLKNPPGILITTPESLelllvnkkLRELFAG------LRYVVVDE 119
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
37-130 |
4.00e-07 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 50.02 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 37 VLEGKNLLAAAQTGTGKTAaFGLpiIQSVQQEKLNGtpKALILVPTRELAQQVFESLSQYASQTAL--RIVCVYGGISIG 114
Cdd:cd17924 29 LLRGKSFAIIAPTGVGKTT-FGL--ATSLYLASKGK--RSYLIFPTKSLVKQAYERLSKYAEKAGVevKILVYHSRLKKK 103
|
90 100
....*....|....*....|
gi 520915635 115 VQKKKLE----DGADILIAT 130
Cdd:cd17924 104 EKEELLEkiekGDFDILVTT 123
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
37-187 |
5.25e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 51.88 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 37 VLEGKNLLAAAQTGTGKTAAFGLPIIQSVqqekLNGTpKALILVPTRELAQQVFESLSQYASQtalrivcvygGISIGVQ 116
Cdd:PRK02362 36 LLDGKNLLAAIPTASGKTLIAELAMLKAI----ARGG-KALYIVPLRALASEKFEEFERFEEL----------GVRVGIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 117 KKKLE-DGA-----DILIATPGRLLDHLFNGNVNISKTNTLVLDE------ADRmldmGfwPDLQRI---LRRLPDEKQI 181
Cdd:PRK02362 101 TGDYDsRDEwlgdnDIIVATSEKVDSLLRNGAPWLDDITCVVVDEvhlidsANR----G--PTLEVTlakLRRLNPDLQV 174
|
....*.
gi 520915635 182 MLFSAT 187
Cdd:PRK02362 175 VALSAT 180
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
29-155 |
5.45e-07 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 50.05 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 29 VQEKSIPHVLEG-KNLLAAAQTGTGKTAAFGLPIIQSVQQEKLN--GTPKALILVPTRELAQQVFESLSQYASQTALRIV 105
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 520915635 106 CVYGGISIGvQKKKLEDgADILIATPGR--LLDHLFNGNVNISKTNTLVL-DE 155
Cdd:cd18023 85 ELTGDTEMD-DTFEIQD-ADIILTTPEKwdSMTRRWRDNGNLVQLVALVLiDE 135
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-187 |
7.36e-07 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 51.36 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 1 MSVNfaDLGIEQNLVETLSTLNIVTPTPVQEKSIPH-VLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlngtPKALIL 79
Cdd:PRK00254 1 MKVD--ELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREG----GKAVYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 80 VPTRELAQQVFESLSQYaSQTALRIVCVYGGISigvQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRM 159
Cdd:PRK00254 75 VPLKALAEEKYREFKDW-EKLGLRVAMTTGDYD---STDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLI 150
|
170 180
....*....|....*....|....*...
gi 520915635 160 LDMGFWPDLQRILRRLPDEKQIMLFSAT 187
Cdd:PRK00254 151 GSYDRGATLEMILTHMLGRAQILGLSAT 178
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
25-130 |
1.00e-06 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part 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: 350676 [Multi-domain] Cd Length: 180 Bit Score: 48.57 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 25 TPTPVQEKSIPHVL------EGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKlngtpKALILVPTRELAQQVFESLSQYAS 98
Cdd:cd17918 15 SLTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGAALLAYKNGK-----QVAILVPTEILAHQHYEEARKFLP 89
|
90 100 110
....*....|....*....|....*....|..
gi 520915635 99 QtaLRIVCVYGGisigvQKKKLEDGADILIAT 130
Cdd:cd17918 90 F--INVELVTGG-----TKAQILSGISLLVGT 114
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
202-340 |
1.03e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 48.03 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 202 SPVEIEVTPPNT--TAETVTQIVYPVDKKRKrellayligsknwqqVLVFTKTKQGSDELAKELK------LDGIKAVSI 273
Cdd:cd18796 10 LPVAPEIFPWAGesGADAYAEVIFLLERHKS---------------TLVFTNTRSQAERLAQRLRelcpdrVPPDFIALH 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520915635 274 NGDKSQGARQRALDEFKQGKVRALIATDVAARGLDIQELEQVINFDMPFKAEDYVHRIGRTGRAGNS 340
Cdd:cd18796 75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGA 141
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
49-188 |
3.42e-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: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 49 TGTGKTAaFGLPIIQsvqqekLNGTPKALILVPTRELAQQVFESLSQYASQTALRIvcvyggisIGVQKKKLEDGADILI 128
Cdd:cd17926 27 TGSGKTL-TALALIA------YLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGL--------IGGGKKKDFDDANVVV 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 129 ATPGRLLDHLFNGNVNISKTNTLVLDEADRmLDMGFWpdlQRILRRLPDEKQiMLFSATF 188
Cdd:cd17926 92 ATYQSLSNLAEEEKDLFDQFGLLIVDEAHH-LPAKTF---SEILKELNAKYR-LGLTATP 146
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
25-155 |
2.22e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 45.16 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 25 TPTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQEKLNGTP-KALILVPTRELAQQVFESLSQYASQtALR 103
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKgRVVVLVNKVPLVEQQLEKFFKYFRK-GYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 520915635 104 IVCVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVN----ISKTNTLVLDE 155
Cdd:cd18036 81 VTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
26-187 |
3.71e-05 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 44.18 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 26 PTPVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIQSVQQeklngTPKALILVPTRELAQQVFESLSQyasqtalriv 105
Cdd:cd18027 9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKH-----MTRTIYTSPIKALSNQKFRDFKN---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 106 cVYGGISIGVQKKKLEDGADILIATPGRLLDHLFNGNVNISKTNTLVLDEADRMLDMGFWPDLQRILRRLPDEKQIMLFS 185
Cdd:cd18027 74 -TFGDVGLITGDVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLS 152
|
..
gi 520915635 186 AT 187
Cdd:cd18027 153 AT 154
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
223-344 |
4.35e-05 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 43.40 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 223 YPVDKKRKRE--------LLAYLIGSKnwQQVLVFTKTKQGSDELAKELKlDGIKAVSINGDKSQGAR-------QRAL- 286
Cdd:cd18797 9 LLDRKDGERGsarreaarLFADLVRAG--VKTIVFCRSRKLAELLLRYLK-ARLVEEGPLASKVASYRagylaedRREIe 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 520915635 287 DEFKQGKVRALIATDVAARGLDIQELEQVINFDMPFKAEDYVHRIGRTGRAGNSGLAV 344
Cdd:cd18797 86 AELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
222-382 |
4.64e-05 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 43.83 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 222 VYPVDKKRKRELLAYL--IGSKnwqqVLVFTKT---KQGSDELAKELKLDGIKAVSINGDksqgaRQRALDEFKQGKVRA 296
Cdd:cd18798 5 VYIEDSDSLEKLLELVkkLGDG----GLIFVSIdygKEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 297 LIAT----DVAARGLDIQE-LEQVINFDMPfkAEDYVHRIGRTGR--AGNSGLAVSLMSRDEEYLLHAIENLLDQRLPQE 369
Cdd:cd18798 76 LIGVasyyGVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRlyAGGLTKGLSVVLVDDPELFEALKKRLKLILDEF 153
|
170
....*....|...
gi 520915635 370 WLAGFEPSLIEEV 382
Cdd:cd18798 154 IFKELEEVDLEEL 166
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
25-62 |
5.46e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 45.65 E-value: 5.46e-05
10 20 30
....*....|....*....|....*....|....*....
gi 520915635 25 TPTPVQEKSIPHVLEGKNLLAAAQTGTGKT-AAFgLPII 62
Cdd:PRK13767 32 TFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAII 69
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
247-316 |
8.08e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 41.78 E-value: 8.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520915635 247 LVFTKTKQGSDELAKELKLDGIKAVSINGDKSQ---GARQRALDEFKQGKVRALIATDVAARGLDIQELEQVI 316
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDrerGDEALILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
23-189 |
1.03e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 42.66 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 23 IVTPTPVQEKSIPHVLEG-----KNLLAAAQTGTGKT--AAFglpIIQSVQQEklNGTPKALILVPTRELAQQVFESLSQ 95
Cdd:pfam04851 1 KLELRPYQIEAIENLLESikngqKRGLIVMATGSGKTltAAK---LIARLFKK--GPIKKVLFLVPRKDLLEQALEEFKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 96 YASqtalriVCVYGGISIGVQKKKLE-DGADILIATPGRLLDHLFNGNVNISKTNTLVL--DEADRMLDMGFwpdlQRIL 172
Cdd:pfam04851 76 FLP------NYVEIGEIISGDKKDESvDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHRSGASSY----RNIL 145
|
170
....*....|....*..
gi 520915635 173 RRLPdEKQIMLFSATFE 189
Cdd:pfam04851 146 EYFK-PAFLLGLTATPE 161
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
28-187 |
5.46e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 40.98 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 28 PVQEKSIPHVLEGKNLLAAAQTGTGKTAAFGLPIIqsvqqeKLNGTpkALILVPTRELAQ-QVfESLsqyaSQTALRIVC 106
Cdd:cd17920 15 PGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL------LLDGV--TLVVSPLISLMQdQV-DRL----QQLGIRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 107 VYGGISIGVQKK---KLEDG-ADILIATPGRLLDHLFNGNVNISKTNT----LVLDEADRMLDMG--FWPDLQRI--LRR 174
Cdd:cd17920 82 LNSTLSPEEKREvllRIKNGqYKLLYVTPERLLSPDFLELLQRLPERKrlalIVVDEAHCVSQWGhdFRPDYLRLgrLRR 161
|
170
....*....|...
gi 520915635 175 LPDEKQIMLFSAT 187
Cdd:cd17920 162 ALPGVPILALTAT 174
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
38-155 |
3.19e-03 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 38.65 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 38 LEGKNLLAAAQTGTGKTaaFGLPIIQSVQQEKLNGTPKALIL-----VPTRELAQQVFeslSQYASQTALRIVCVYGGIS 112
Cdd:cd18073 15 MKGKNTIICAPTGCGKT--FVSLLICEHHLKKFPQGQKGKVVffatkVPVYEQQKSVF---SKYFERHGYRVTGISGATA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 520915635 113 IGVQKKKLEDGADILIATPGRLLDHLFNGNV-NISKTNTLVLDE 155
Cdd:cd18073 90 ENVPVEQIIENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 133
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
43-309 |
6.04e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 38.56 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 43 LLAAAQTGTGKTAAFGLPIIQSVQQEKLNgtpKALILVPTRELAQQVFESLSQYASQTALrivcvyGGISIGVQKKKLED 122
Cdd:cd09639 2 LVIEAPTGYGKTEAALLWALHSLKSQKAD---RVIIALPTRATINAMYRRAKEAFGETGL------YHSSILSSRIKEMG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 123 --------------GADILIATP-------------GRLLDHLFNGNVNISKTNtLVLDEADRMLD--MGFwpdLQRILR 173
Cdd:cd09639 73 dseefehlfplyihSNDTLFLDPitvctidqvlksvFGEFGHYEFTLASIANSL-LIFDEVHFYDEytLAL---ILAVLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 174 RLPDEKQ-IMLFSATFEKRIKTIAYKlMDSPVEIEVTPPNTTAETVTQIVYPVDKKRKRELLAYLIGSKNWQQVLVFTKT 252
Cdd:cd09639 149 VLKDNDVpILLMSATLPKFLKEYAEK-IGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGSVAIIVNT 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520915635 253 KQGSDELAKELKLDG--IKAVSINGDKSQGARQRA----LDEFKQGKVRALIATDVAARGLDI 309
Cdd:cd09639 228 VDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
28-187 |
8.05e-03 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain] Cd Length: 200 Bit Score: 37.53 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 28 PVQEKSIPHVLEGKNLLAAAQTGTGKTAAfGLPIIQSVQQEKLNGtpKALILVPTRELAQQVFESLSQYASQtALRIVCV 107
Cdd:cd18075 5 GYQWEVVAPALRGKNSIIWLPTGAGKTRA-AVYVARRHLETKRGA--KVAVLVNKVHLVDQHLEKEFHVLLD-KYTVTAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 108 YGGISIGVQKKKLEDGADILIATPGRLLDHLFNGN----VNISKTNTLVLDEA-----DRMLDMGFWPDLQRILRRLPDE 178
Cdd:cd18075 81 SGDSSHKCFFGQLARGSDVVICTAQILQNALLSGEeeahVELTDFSLLVIDEChhthkEAVYNKIMLSYLEKKLSRQGDL 160
|
....*....
gi 520915635 179 KQIMLFSAT 187
Cdd:cd18075 161 PQILGLTAS 169
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
41-130 |
8.44e-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: 36.77 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520915635 41 KNLLAAAqTGTGKT--AAFglpIIQSVQQEklNGTPKALILVPTRELAQQVFESLSQyasqtalrivcVYGGISIGV--Q 116
Cdd:cd18032 22 RALLVMA-TGTGKTytAAF---LIKRLLEA--NRKKRILFLAHREELLEQAERSFKE-----------VLPDGSFGNlkG 84
|
90
....*....|....
gi 520915635 117 KKKLEDGADILIAT 130
Cdd:cd18032 85 GKKKPDDARVVFAT 98
|
|
| |
