|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-429 |
0e+00 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 943.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 2 KKTHITEQKFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQ 81
Cdd:PRK04837 1 SKTHLTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 82 PTQPRAIIMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQA 161
Cdd:PRK04837 81 VNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 162 VVLDEADRMFDLGFIKDIRFLFRRMPAPQERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKTGHRIQEELFYPSNE 241
Cdd:PRK04837 161 VVLDEADRMFDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 242 DKMALLQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLH 321
Cdd:PRK04837 241 EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 322 IPQVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEYIEHTIPVSDYDSNALIPDLPAPVRTps 401
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYDSDALLTDLPKPLRL-- 398
|
410 420
....*....|....*....|....*...
gi 516400179 402 srnQQRRTNTGGARSGDRKSNNRRPRQP 429
Cdd:PRK04837 399 ---TRPRTGNGPRRSGAPRNRRRRKRSG 423
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
10-435 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 542.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 10 KFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHegrqptQPRAII 89
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR------APQALI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 90 MAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADR 169
Cdd:COG0513 77 LAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 170 MFDLGFIKDIRFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKTGHRIQEELFYPSNEDKMALLQT 249
Cdd:COG0513 157 MLDMGFIEDIERILKLLPK--ERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 250 LIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHVF 329
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 330 NYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEYIEHTIPVSDYDSNALIPDLPAPVRTPSSRNQQRRT 409
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGK 394
|
410 420
....*....|....*....|....*.
gi 516400179 410 NTGGARSGDRKSNNRRPRQPRQHKEA 435
Cdd:COG0513 395 KAGRGGRPGPKGERKARRGKRRRRKR 420
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-435 |
1.22e-174 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 500.63 E-value: 1.22e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 1 MKKTHITEQKFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGR 80
Cdd:PRK04537 1 MSDKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 81 QPTQPRAIIMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQ-RVFNLNNI 159
Cdd:PRK04537 81 KPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 160 QAVVLDEADRMFDLGFIKDIRFLFRRMPAPQERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKTGHRIQEELFYPS 239
Cdd:PRK04537 161 EICVLDEADRMFDLGFIKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 240 NEDKMALLQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARG 319
Cdd:PRK04537 241 DEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 320 LHIPQVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEYIEHTIPVSDYDSNALIPdLPAPVRT 399
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELLTP-LPRPPRV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516400179 400 PS-------------------SRNQ-----QRRtntGGARSGDRKS-------------------NNRRPRQPRQHKEA 435
Cdd:PRK04537 400 PVegeeaddeagdsvgtifreAREQraaeeQRR---GGGRSGPGGGsrsgsvggggrrdgagadgKPRPRRKPRVEGEA 475
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
10-391 |
3.61e-125 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 371.17 E-value: 3.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 10 KFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPTQPRAII 89
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 90 MAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGG-VDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEAD 168
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 169 RMFDLGFIKDIRFLFRRMPAPQERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKTGHRIQEELFYPSNEDKMALLQ 248
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 249 TLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHV 328
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516400179 329 FNYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEYIEHTIPVSDYDSNALIP 391
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELLKP 470
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
11-379 |
2.62e-102 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 311.11 E-value: 2.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAhegRQPTQPRAIIM 90
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPR---RKSGPPRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRM 170
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 171 FDLGFIKDIRFLfrrmpAPQERL---NMLFSATLSYR-VQELAFEHMHNPEHVVVEPEQKTGHRIQEelFY---PSNEDK 243
Cdd:PRK11192 160 LDMGFAQDIETI-----AAETRWrkqTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQ--WYyraDDLEHK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 244 MALLQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIP 323
Cdd:PRK11192 233 TALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 516400179 324 QVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFA-CEDYAInLPAIEEYIEHTI 379
Cdd:PRK11192 313 DVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVeAHDHLL-LGKIERYIEEPL 368
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
11-428 |
1.07e-97 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 300.19 E-value: 1.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAH-EGRQPTqpRAII 89
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHaKGRRPV--RALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 90 MAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADR 169
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 170 MFDLGFIKDIRFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKTGHRIQEELFYPSNEDKMALLQT 249
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPA--KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 250 LIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHVF 329
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 330 NYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEYIEHTIP---VSDYDsnaliPDlPAPVRTPSSRNQQ 406
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPriaIPGYE-----PD-PSIKAEPIQNGRQ 392
|
410 420
....*....|....*....|..
gi 516400179 407 RRTNTGGARSGDRKSNNRRPRQ 428
Cdd:PRK10590 393 QRGGGGRGQGGGRGQQQGQPRR 414
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
11-399 |
2.29e-97 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 299.41 E-value: 2.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLlttpahegrQPTQPR--AI 88
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL---------DVKRFRvqAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 89 IMAPTRELAIQIYNDAEPLI-ASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEA 167
Cdd:PRK11776 77 VLCPTRELADQVAKEIRRLArFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 168 DRMFDLGFIKDIRFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNPEHVVVEpEQKTGHRIqEELFYP-SNEDKMAL 246
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPA--RRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAI-EQRFYEvSPDERLPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 247 LQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVT 326
Cdd:PRK11776 233 LQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516400179 327 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEYIEHTIPVSDYDSNALIPDLP--APVRT 399
Cdd:PRK11776 313 AVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPllPEMVT 387
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
20-219 |
7.81e-90 |
|
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: 270.47 E-value: 7.81e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPtqpRAIIMAPTRELAIQ 99
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGP---QALVLAPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDI 179
Cdd:cd00268 78 IAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 516400179 180 RFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNPEHV 219
Cdd:cd00268 158 EKILSALPK--DRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
10-426 |
1.51e-81 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 261.25 E-value: 1.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 10 KFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHegRQPTQPRAII 89
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLL--RYGDGPIVLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 90 MAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADR 169
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 170 MFDLGFIKDIRFLFRRM-PapqERLNMLFSATLSYRVQELAFEHM-HNPEHVVVEP-EQKTGHRIQEELFYPSNEDKMAL 246
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIrP---DRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSlDLTACHNIKQEVFVVEEHEKRGK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 247 LQTLIEEEWPD--RAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQ 324
Cdd:PTZ00110 366 LKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKD 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 325 VTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFACED---YAINLPAIEEYIEHTIPvsdydsnaliPDLpAPVRTPS 401
Cdd:PTZ00110 446 VKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDkyrLARDLVKVLREAKQPVP----------PEL-EKLSNER 514
|
410 420
....*....|....*....|....*
gi 516400179 402 SRNQQRRTNTGGARSGDrkSNNRRP 426
Cdd:PTZ00110 515 SNGTERRRWGGYGRFSN--NVNNIP 537
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
7-380 |
5.48e-78 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 254.00 E-value: 5.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 7 TEQKFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAhegrqptQPR 86
Cdd:PRK11634 4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELK-------APQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 87 AIIMAPTRELAIQIyndAEPLIAST----GIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAV 162
Cdd:PRK11634 77 ILVLAPTRELAVQV---AEAMTDFSkhmrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 163 VLDEADRMFDLGFIKDIRFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKTGHRIQEELFYPSNED 242
Cdd:PRK11634 154 VLDEADEMLRMGFIEDVETIMAQIPE--GHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 243 KMALLQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHI 322
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 516400179 323 PQVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEYIEHTIP 380
Cdd:PRK11634 312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIP 369
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
11-215 |
1.04e-71 |
|
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: 225.06 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHE---GRQPTQPRA 87
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 88 IIMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEA 167
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 516400179 168 DRMFDLGFIKDIRFLFRR--MPAPQERLNMLFSATLSYRVQELAFEHMHN 215
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdMPPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
11-374 |
5.64e-66 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 216.23 E-value: 5.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNhlLTTPAHEGRQptqprAIIM 90
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQ--LIDYDLNACQ-----ALIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRM 170
Cdd:PTZ00424 103 APTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 171 FDLGFIKDIRFLFRRMPapQERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKTGHRIQEelFY---PSNEDKMALL 247
Cdd:PTZ00424 183 LSRGFKGQIYDVFKKLP--PDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ--FYvavEKEEWKFDTL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 248 QTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTH 327
Cdd:PTZ00424 259 CDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 516400179 328 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISFACEDYAINLPAIEEY 374
Cdd:PTZ00424 339 VINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERH 385
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-363 |
2.70e-59 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 201.94 E-value: 2.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPTQPRAIIM 90
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRM 170
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 171 FDLGFIKDIRFLFRRMPAPQErlnMLFSATLSYRVQELAFEHMHNPEHVVV-EPEQKTGHRIQEELFYPSNEDKMALLQT 249
Cdd:PLN00206 283 LERGFRDQVMQIFQALSQPQV---LLFSATVSPEVEKFASSLAKDIILISIgNPNRPNKAVKQLAIWVETKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 250 LI-EEEWPDRAIIFANTKykcesIWAHLAADGHRV--GL----LTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHI 322
Cdd:PLN00206 360 LKsKQHFKPPAVVFVSSR-----LGADLLANAITVvtGLkalsIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 516400179 323 PQVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFACED 363
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
5-214 |
1.04e-56 |
|
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: 187.87 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 5 HITEqkFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTT--PAHEGRQP 82
Cdd:cd18052 41 AILT--FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEglTASSFSEV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 83 TQPRAIIMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAV 162
Cdd:cd18052 119 QEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516400179 163 VLDEADRMFDLGFIKDIRFL--FRRMPAPQERLNMLFSATLSYRVQELAFEHMH 214
Cdd:cd18052 199 ILDEADRMLDMGFGPEIRKLvsEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
33-208 |
2.58e-56 |
|
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: 183.21 E-value: 2.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 33 TPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHegrqptqPRAIIMAPTRELAIQIYNDAEPLIASTG 112
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG-------PQALVLAPTRELAEQIYEELKKLGKGLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 113 IKAALAYGGESYDKQLAKLQgGVDVLIGTTGRIIDFYKQRVfNLNNIQAVVLDEADRMFDLGFIKDIRFLFRRMpaPQER 192
Cdd:pfam00270 74 LKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL--PKKR 149
|
170
....*....|....*.
gi 516400179 193 LNMLFSATLSYRVQEL 208
Cdd:pfam00270 150 QILLLSATLPRNLEDL 165
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
9-216 |
5.50e-56 |
|
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: 184.50 E-value: 5.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 9 QKFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRqpTQPRAI 88
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPG--EGPIGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 89 IMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFY---KQRVFNLNNIQAVVLD 165
Cdd:cd17953 90 IMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516400179 166 EADRMFDLGF-------IKDIRflfrrmpapQERLNMLFSATLSYRVQELAFEHMHNP 216
Cdd:cd17953 170 EADRMFDMGFepqimkiVNNIR---------PDRQTVLFSATFPRKVEALARKVLHKP 218
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
238-359 |
1.79e-55 |
|
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: 180.01 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 238 PSNEDKMALLQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAA 317
Cdd:cd18787 9 EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 516400179 318 RGLHIPQVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISF 359
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITF 130
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
16-222 |
5.62e-54 |
|
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: 178.93 E-value: 5.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 16 LNPQVVEGLEKKGFEFCTPIQALALPVLLS-GQDIAGQAQTGTGKTLAFLTATFNHLLTTPahEGRQPTQPRAIIMAPTR 94
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTK--PAGRRSGVSALIISPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 95 ELAIQIYNDAEPLIA-STGIKAALAYGGESYDKQLAKLQ-GGVDVLIGTTGRIID-FYKQRVFN-LNNIQAVVLDEADRM 170
Cdd:cd17964 79 ELALQIAAEAKKLLQgLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDhLENPGVAKaFTDLDYLVLDEADRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516400179 171 FDLGFIKDIRFLFRRMPAPQE--RLNMLFSATLSYRVQELAFEHMhNPEHVVVE 222
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEKNAdpRQTLLFSATVPDEVQQIARLTL-KKDYKFID 211
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
20-219 |
7.00e-53 |
|
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: 175.52 E-value: 7.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPahegRQPTQPRAIIMAPTRELAIQ 99
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRP----KKKAATRVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQ-RVFNLNNIQAVVLDEADRMFDLGFIKD 178
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516400179 179 IRFLFRRMpaPQERLNMLFSATLSYRVQELAFEHMHNPEHV 219
Cdd:cd17947 157 LKEILRLC--PRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
20-220 |
1.87e-51 |
|
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: 171.83 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQptQPRAIIMAPTRELAIQ 99
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGE--GPIAVIVAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDI 179
Cdd:cd17952 79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 516400179 180 RFLFRRM-PapqERLNMLFSATLSYRVQELAFEHMHNPEHVV 220
Cdd:cd17952 159 RSIVGHVrP---DRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
20-219 |
7.19e-51 |
|
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: 171.35 E-value: 7.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPTQ-PRAIIMAPTRELAI 98
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDgPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 99 QIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKD 178
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516400179 179 IRFLFRRMPAPQE------------------RLNMLFSATLSYRVQELAFEHMHNPEHV 219
Cdd:cd17945 161 VTKILDAMPVSNKkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
11-219 |
7.40e-51 |
|
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: 170.58 E-value: 7.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPahegrqptQP-RAII 89
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP--------QRfFALV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 90 MAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQ-RVFNLNNIQAVVLDEAD 168
Cdd:cd17954 74 LAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEAD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516400179 169 RMFDLGFIKDIRFLFRRMpaPQERLNMLFSATLSYRVQELAFEHMHNPEHV 219
Cdd:cd17954 154 RLLNMDFEPEIDKILKVI--PRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
11-219 |
1.25e-50 |
|
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: 170.18 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLlttPAHEGRqpTQPRAIIM 90
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPT--VGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRM 170
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516400179 171 FDLGFIKDIRFLFRRMPAPQERLnmLFSATLSYRVQELAFEHMHNPEHV 219
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTL--LFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
20-220 |
1.02e-49 |
|
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: 167.37 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTtpAHEGRQPTQPRAIIMAPTRELAIQ 99
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK--RKANLKKGQVGALIISPTRELATQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLIASTG--IKAALAYGGESYDKQLAKL-QGGVDVLIGTTGRIIDFY--KQRVFNLNNIQAVVLDEADRMFDLG 174
Cdd:cd17960 79 IYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLsrKADKVKVKSLEVLVLDEADRLLDLG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516400179 175 FIKDIRFLFRRMpaPQERLNMLFSATLSYRVQELAFEHMHNPEHVV 220
Cdd:cd17960 159 FEADLNRILSKL--PKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
24-221 |
4.45e-48 |
|
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: 163.14 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 24 LEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGrqptqPRAIIMAPTRELAIQIYND 103
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKG-----LRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 104 AEPLIASTGIKAALAYGGESyDKQLAKLQGG--VDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDIRF 181
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLE-AKAKDGPKSItkYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 516400179 182 LFRRMPAPQERLnMLFSATLSYRVQELAFEHMHNPEHVVV 221
Cdd:cd17957 159 ILAACTNPNLQR-SLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
20-220 |
3.99e-47 |
|
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: 160.71 E-value: 3.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPTqPRAIIMAPTRELAIQ 99
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNG-PGVLVLTPTRELALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLiASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDI 179
Cdd:cd17958 80 IEAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 516400179 180 R-FLFRRMPapqERLNMLFSATLSYRVQELAFEHMHNPEHVV 220
Cdd:cd17958 159 RkILLDIRP---DRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
24-234 |
5.68e-47 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 160.35 E-value: 5.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 24 LEKKGFEFCTPIQALALPVLLSG-QDIAGQAQTGTGKTLAFLTATFNHLLTTPAhegrqptqPRAIIMAPTRELAIQIYN 102
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG--------GRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 103 DAEPLIASTGIKAALAYGGESYDKQLAKLQGGV-DVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDIRF 181
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516400179 182 LFRRMPAPQERLnmLFSATLSYRVQELAFEHMHNPehVVVEPEQKTGHRIQEE 234
Cdd:smart00487 153 LLKLLPKNVQLL--LLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
20-220 |
6.23e-47 |
|
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: 160.23 E-value: 6.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHegRQPTQPRAIIMAPTRELAIQ 99
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPL--ERGDGPIVLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDI 179
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516400179 180 RFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNPEHVV 220
Cdd:cd17966 159 RKIVDQIRP--DRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
20-220 |
3.48e-45 |
|
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: 156.21 E-value: 3.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKK-GFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQpTQPRAIIMAPTRELAI 98
Cdd:cd17949 1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRS-DGTLALVLVPTRELAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 99 QIYNDAEPLI-ASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQ-RVFNLNNIQAVVLDEADRMFDLGFI 176
Cdd:cd17949 80 QIYEVLEKLLkPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516400179 177 KDIRFLFRRM-----------PAPQERLNMLFSATLSYRVQELAFEHMHNPEHVV 220
Cdd:cd17949 160 KDITKILELLddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
11-216 |
6.17e-45 |
|
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: 155.15 E-value: 6.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHegrqptqPRAIIM 90
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV-------IQALIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRM 170
Cdd:cd17940 74 VPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516400179 171 FDLGFIKDIRFLFRRMpaPQERLNMLFSATLSYRVQELAFEHMHNP 216
Cdd:cd17940 154 LSQDFQPIIEKILNFL--PKERQILLFSATFPLTVKNFMDRHMHNP 197
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
5-215 |
3.45e-42 |
|
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: 149.42 E-value: 3.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 5 HITEqkFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNH---------LLTTP 75
Cdd:cd18051 19 HIET--FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQiyeqgpgesLPSES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 76 AHEGRQPTQPRAIIMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFN 155
Cdd:cd18051 97 GYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516400179 156 LNNIQAVVLDEADRMFDLGFIKDIRFLFRR--MPAPQERLNMLFSATLSYRVQELAFEHMHN 215
Cdd:cd18051 177 LDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
11-219 |
2.23e-41 |
|
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: 145.54 E-value: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLlttpahegrqptqpRAIIM 90
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV--------------VALIL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPL---IASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEA 167
Cdd:cd17938 67 EPSRELAEQTYNCIENFkkyLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516400179 168 DRMFDLGFIKDIRFLFRRMP---APQERLNM-LFSATL-SYRVQELAFEHMHNPEHV 219
Cdd:cd17938 147 DRLLSQGNLETINRIYNRIPkitSDGKRLQViVCSATLhSFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
23-222 |
3.87e-41 |
|
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: 144.74 E-value: 3.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 23 GLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLttpahegRQPTQPR----AIIMAPTRELAI 98
Cdd:cd17941 4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY-------RERWTPEdglgALIISPTRELAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 99 QIYNDAEPLIASTGIKAALAYGGESYDKQLAKLqGGVDVLIGTTGRIIDFYKQRV-FNLNNIQAVVLDEADRMFDLGFIK 177
Cdd:cd17941 77 QIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 516400179 178 DIRFLFRRMpaPQERLNMLFSATLSYRVQELAFEHMHNPEHVVVE 222
Cdd:cd17941 156 TLDAIVENL--PKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
20-202 |
6.43e-41 |
|
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: 145.46 E-value: 6.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPV-LLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPTQ--PRAIIMAPTREL 96
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 97 AIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAV---VLDEADRMFDL 173
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 516400179 174 GFIKDIRFLFRRMPAPQE-----RLNMLFSATLS 202
Cdd:cd17946 161 GHFAELEKILELLNKDRAgkkrkRQTFVFSATLT 194
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
11-216 |
4.31e-40 |
|
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: 142.36 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLlttpaheGRQPTQPRAIIM 90
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL-------SEDPYGIFALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYK---QRVFNLNNIQAVVLDEA 167
Cdd:cd17955 74 TPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516400179 168 DRMFDLGFIKDIRFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNP 216
Cdd:cd17955 154 DRLLTGSFEDDLATILSALPP--KRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
21-209 |
5.28e-40 |
|
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: 141.73 E-value: 5.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 21 VEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFnHLLTTPAHEGRQPTQprAIIMAPTRELAIQI 100
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-ELLYKLKFKPRNGTG--VIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 101 YNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRV-FNLNNIQAVVLDEADRMFDLGFIKDI 179
Cdd:cd17942 79 YGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgFLYKNLQCLIIDEADRILEIGFEEEM 158
|
170 180 190
....*....|....*....|....*....|
gi 516400179 180 RFLFRRMpaPQERLNMLFSATLSYRVQELA 209
Cdd:cd17942 159 RQIIKLL--PKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
24-216 |
9.07e-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: 138.45 E-value: 9.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 24 LEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTtpahegrQPTQPRAIIMAPTRELAIQIYND 103
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT-------EHRNPSALILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 104 AEPLIAST-GIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDIRFL 182
Cdd:cd17962 78 AKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157
|
170 180 190
....*....|....*....|....*....|....
gi 516400179 183 FRRMPAPQERLnmLFSATLSYRVQELAFEHMHNP 216
Cdd:cd17962 158 LENISHDHQTI--LVSATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
20-209 |
1.95e-38 |
|
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: 137.86 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFltaTFNHLLTTPAHEGRQPTQ----PRAIIMAPTRE 95
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVF---TLPLIMFALEQEKKLPFIkgegPYGLIVCPSRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 96 LAIQIYNDAEPLIAS------TGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADR 169
Cdd:cd17951 78 LARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 516400179 170 MFDLGFIKDIRFLFRRMPAPqeRLNMLFSATLSYRVQELA 209
Cdd:cd17951 158 MIDMGFEEDIRTIFSYFKGQ--RQTLLFSATMPKKIQNFA 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
20-219 |
1.49e-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: 135.08 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLttpahegRQPTQPRAIIMAPTRELAIQ 99
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD-------LERRHPQVLILAPTREIAVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLIAS-TGIKAALAYGGESYDKQLAKLqGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKD 178
Cdd:cd17943 74 IHDVFKKIGKKlEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516400179 179 IRFLFRRMPAPQERLnmLFSATLSYRVQELAFEHMHNPEHV 219
Cdd:cd17943 153 VNWIFSSLPKNKQVI--AFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
13-216 |
1.80e-37 |
|
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: 135.14 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 13 DLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPahegrqpTQPRAIIMAP 92
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV-------RETQALVLAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 93 TRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFD 172
Cdd:cd17939 74 TRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 516400179 173 LGFIKDIRFLFRRMpaPQERLNMLFSATLSYRVQELAFEHMHNP 216
Cdd:cd17939 154 RGFKDQIYDIFQFL--PPETQVVLFSATMPHEVLEVTKKFMRDP 195
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
16-209 |
3.68e-37 |
|
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: 134.24 E-value: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 16 LNPQVVEGLEKKGFEFCTPIQALALPVLLSG--QDIAGQAQTGTGKTLAFLTATFNHLLTTPAHegrqptqPRAIIMAPT 93
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKS-------PQALCLAPT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 94 RELAIQIYNDAEPLIASTGIKAALAY-GGESYDKQLAKLQggvdVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFD 172
Cdd:cd17963 74 RELARQIGEVVEKMGKFTGVKVALAVpGNDVPRGKKITAQ----IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLD 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 516400179 173 L-GFIKDIRFLFRRMPAPQERLnmLFSATLSYRVQELA 209
Cdd:cd17963 150 TqGHGDQSIRIKRMLPRNCQIL--LFSATFPDSVRKFA 185
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
10-221 |
1.64e-36 |
|
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: 133.98 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 10 KFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEgrQPTQPRAII 89
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLE--RGDGPICLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 90 MAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADR 169
Cdd:cd18049 103 LAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516400179 170 MFDLGFIKDIRFLFRRMPApqERLNMLFSATLSYRVQELAFEHMHNPEHVVV 221
Cdd:cd18049 183 MLDMGFEPQIRKIVDQIRP--DRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
16-216 |
1.74e-35 |
|
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: 130.01 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 16 LNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPtQPRAIIMAPTRE 95
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQ-GTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 96 LAIQIYNDAEPLIASTG--IKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQ-RVFNLNNIQAVVLDEADRMFD 172
Cdd:cd17961 80 LAQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESgSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 516400179 173 LGFIKDIRFLFRRMP-APQerlNMLFSATLSYRVQELAFEHMHNP 216
Cdd:cd17961 160 YGYEEDLKSLLSYLPkNYQ---TFLMSATLSEDVEALKKLVLHNP 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
242-351 |
9.36e-35 |
|
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: 125.02 E-value: 9.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 242 DKMALLQTLIEEEWPDRAIIFANTKYKCESIWaHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLH 321
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 516400179 322 IPQVTHVFNYDLPDDCEDYVHRIGRTGRAG 351
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
24-213 |
1.18e-34 |
|
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: 127.66 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 24 LEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLlttpaHEGRQPTQ----PRAIIMAPTRELAIQ 99
Cdd:cd17944 5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL-----QEDQQPRKrgraPKVLVLAPTRELANQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLiaSTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGF---I 176
Cdd:cd17944 80 VTKDFKDI--TRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFaeqV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 516400179 177 KDIRFLFRRMPAPQERLNMLFSATLSYRVQELAFEHM 213
Cdd:cd17944 158 EEILSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
18-209 |
4.68e-34 |
|
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: 128.20 E-value: 4.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 18 PQ-VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEgrQPTQPRAIIMAPTREL 96
Cdd:cd18050 70 PQyVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLE--RGDGPICLVLAPTREL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 97 AIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFI 176
Cdd:cd18050 148 AQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFE 227
|
170 180 190
....*....|....*....|....*....|...
gi 516400179 177 KDIRFLFRRMPApqERLNMLFSATLSYRVQELA 209
Cdd:cd18050 228 PQIRKIVDQIRP--DRQTLMWSATWPKEVRQLA 258
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
11-221 |
3.91e-33 |
|
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: 123.99 E-value: 3.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTpahegrqPTQPRAIIM 90
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPV-------DGQVSVLVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIAS-TGIKAALAYGGESYDKQLAKLQGGV-DVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEAD 168
Cdd:cd17950 77 CHTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516400179 169 RMF-DLGFIKDIRFLFRRmpAPQERLNMLFSATLSYRVQELAFEHMHNPEHVVV 221
Cdd:cd17950 157 KMLeQLDMRRDVQEIFRA--TPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
11-216 |
6.61e-33 |
|
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: 122.94 E-value: 6.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHegrqptqPRAIIM 90
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA-------TQALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRM 170
Cdd:cd18046 74 APTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516400179 171 FDLGFIKDIRFLFRRMpaPQERLNMLFSATLSYRVQELAFEHMHNP 216
Cdd:cd18046 154 LSRGFKDQIYDIFQKL--PPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
20-208 |
1.14e-31 |
|
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: 120.55 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPAHEGRQPTQPRAIIMAPTRELAIQ 99
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 100 IYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRMFDLGFIKDI 179
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 516400179 180 RFLFRRMP------APQERLNM-----LFSATLSYRVQEL 208
Cdd:cd17948 161 SHFLRRFPlasrrsENTDGLDPgtqlvLVSATMPSGVGEV 200
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
11-216 |
1.19e-30 |
|
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: 116.80 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 11 FADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPahegrqpTQPRAIIM 90
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQV-------RETQALIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEADRM 170
Cdd:cd18045 74 SPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516400179 171 FDLGFIKDIRFLFRRMP-APQerlNMLFSATLSYRVQELAFEHMHNP 216
Cdd:cd18045 154 LNKGFKEQIYDVYRYLPpATQ---VVLVSATLPQDILEMTNKFMTDP 197
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
270-351 |
1.07e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 102.29 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 270 ESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHVFNYDLPDDCEDYVHRIGRTGR 349
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 516400179 350 AG 351
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
20-220 |
1.31e-26 |
|
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: 106.95 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 20 VVEGLEKKGFEFCTPIQALALPVLLSGQ---------DIAGQAQTGTGKTLAFLTATFNHLLTTPAHegrqptQPRAIIM 90
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQALSKRVVP------RLRALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 91 APTRELAIQIYNDAEPLIASTGIKAALAYGGESYDKQLAKLQGG--------VDVLIGTTGRIID-FYKQRVFNLNNIQA 161
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLKHLRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 162 VVLDEADRMFDLGF---------------------IKDIRFLFRRMPAPQErlnMLFSATLSYRVQELAFEHMHNPEHVV 220
Cdd:cd17956 155 LVIDEADRLLNQSFqdwletvmkalgrptapdlgsFGDANLLERSVRPLQK---LLFSATLTRDPEKLSSLKLHRPRLFT 231
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
9-227 |
3.58e-21 |
|
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: 91.62 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 9 QKFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSG--QDIAGQAQTGTGKTLAFLTATFNHLlttpaheGRQPTQPR 86
Cdd:cd18048 18 KSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV-------DALKLYPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 87 AIIMAPTRELAIQIYNDAEPLIA-STGIKAALAYGGESYDK--QLAKlqggvDVLIGTTGRIIDF-YKQRVFNLNNIQAV 162
Cdd:cd18048 91 CLCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGNRPGKgtDIEA-----QIVIGTPGTVLDWcFKLRLIDVTNISVF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516400179 163 VLDEADRMFDLGFIKDIRFLFRRmPAPQERLNMLFSATLSYRVQELAFEHMHNPEHVVVEPEQKT 227
Cdd:cd18048 166 VLDEADVMINVQGHSDHSVRVKR-SMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
33-202 |
1.37e-20 |
|
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: 90.51 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 33 TPIQALALPVLLsGQDIAGQ-----------------AQTGTGKTLAFLTATFNHL---------LTTPAHEG-RQPTQP 85
Cdd:cd17965 32 SPIQTLAIKKLL-KTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLkrqeqepfeEAEEEYESaKDTGRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 86 RAIIMAPTRELAIQIYNDAEPL--IASTGIKAALAYGGESYDKQLAKLQGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVV 163
Cdd:cd17965 111 RSVILVPTHELVEQVYSVLKKLshTVKLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516400179 164 LDEADRMFDLGFIKDIRFLFRRMPApqerLNMLF--SATLS 202
Cdd:cd17965 191 VDEADTLFDRSFLQDTTSIIKRAPK----LKHLIlcSATIP 227
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
9-223 |
1.42e-17 |
|
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: 80.92 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 9 QKFADLGLNPQVVEGLEKKGFEFCTPIQALALPVLLSG--QDIAGQAQTGTGKTLAFLTATFNHLltTPAHEGRQptqpr 86
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 87 AIIMAPTRELAIQIYNDAEPLiASTGIKAALAYGGESYdkqlaKLQGGV----DVLIGTTGRIIDF-YKQRVFNLNNIQA 161
Cdd:cd18047 74 CLCLSPTYELALQTGKVIEQM-GKFYPELKLAYAVRGN-----KLERGQkiseQIVIGTPGTVLDWcSKLKFIDPKKIKV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516400179 162 VVLDEADRMFDLGFIKDIRFLFRRMpAPQERLNMLFSATLSYRVQELAfehmhnpEHVVVEP 223
Cdd:cd18047 148 FVLDEADVMIATQGHQDQSIRIQRM-LPRNCQMLLFSATFEDSVWKFA-------QKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
55-329 |
1.14e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.91 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 55 TGTGKTLAFLTATfnhllttpaheGRQPTQPRAIIMAPTRELAIQIYNDAEpliasTGIKAALAYGGESydkqlaklQGG 134
Cdd:COG1061 109 TGTGKTVLALALA-----------AELLRGKRVLVLVPRRELLEQWAEELR-----RFLGDPLAGGGKK--------DSD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 135 VDVLIGT----TGRIIDFYKQRVFNLnniqaVVLDEADRMFDLGFIKdirfLFRRMPAPqERLNMlfSATL--------- 201
Cdd:COG1061 165 APITVATyqslARRAHLDELGDRFGL-----VIIDEAHHAGAPSYRR----ILEAFPAA-YRLGL--TATPfrsdgreil 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 202 ---------SYRVQELAFEHM-HNPEHVVV----EPEQKTGHRIQEELFY---PSNEDKMALLQTLIEEE-WPDRAIIFA 263
Cdd:COG1061 233 lflfdgivyEYSLKEAIEDGYlAPPEYYGIrvdlTDERAEYDALSERLREalaADAERKDKILRELLREHpDDRKTLVFC 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516400179 264 NTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHVF 329
Cdd:COG1061 313 SSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
244-357 |
1.42e-14 |
|
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: 70.31 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 244 MALLQTLIEEEWPD---RAIIFANTKYKC---ESIWAHLAADGH--RVGLLTG----------DVPQKKREKILEQFTQG 305
Cdd:cd18802 10 QKLIEILREYFPKTpdfRGIIFVERRATAvvlSRLLKEHPSTLAfiRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 516400179 306 SVDLLVATDVAARGLHIPQVTHVFNYDLPDDCEDYVHRIGRtGRAGASGHSI 357
Cdd:cd18802 90 ELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYIL 140
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
243-352 |
2.74e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 71.68 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 243 KMALLQTLIEEEW----PDRAIIFANTKYKCESIWAHLAADGHRVGLLTGD--------VPQKKREKILEQFTQGSVDLL 310
Cdd:COG1111 336 KLSKLREILKEQLgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516400179 311 VATDVAARGLHIPQVTHVFNYDL-PDDCEdYVHRIGRTGRAGA 352
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPvPSEIR-SIQRKGRTGRKRE 457
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
243-345 |
6.96e-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: 62.49 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 243 KMALLQTLIEE--EWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVD--LLVATDVAAR 318
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 516400179 319 GLHIPQVTHVFNYDLP------DDCEDYVHRIG 345
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
243-347 |
8.64e-12 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 67.17 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 243 KMALLQTLIEE--EWPDRAIIFanTKYK--CESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGS--VDLLVATDVA 316
Cdd:COG0553 534 KLEALLELLEEllAEGEKVLVF--SQFTdtLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAG 611
|
90 100 110
....*....|....*....|....*....|....*..
gi 516400179 317 ARGLHIPQVTHVFNYDLP------DDCEDYVHRIGRT 347
Cdd:COG0553 612 GEGLNLTAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
241-366 |
9.83e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 66.70 E-value: 9.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 241 EDKMALLQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATdvAARGL 320
Cdd:COG0514 215 DDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAFGM 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 516400179 321 HI--PQVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISFAC-EDYAI 366
Cdd:COG0514 293 GIdkPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGpEDVAI 341
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
236-359 |
1.61e-10 |
|
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: 58.76 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 236 FYPSNEDKMALLQTLIEEEWPDRAIIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATdv 315
Cdd:cd18794 10 PKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 516400179 316 AARGLHI--PQVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISF 359
Cdd:cd18794 88 VAFGMGIdkPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
52-200 |
1.91e-10 |
|
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: 58.95 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 52 QAQTGTGKTLAFLTATFNHLLTTPahegrqptqPRAIIMAPTRELAIQIYNDAEPLiASTGIKAALAYGGESYDKQLAKL 131
Cdd:cd00046 7 TAPTGSGKTLAALLAALLLLLKKG---------KKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516400179 132 QGGVDVLIGTTGRIIDFYKQRV-FNLNNIQAVVLDEADRMFDLGF---IKDIRFLFRRMPAPQErlnMLFSAT 200
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRgalILDLAVRKAGLKNAQV---ILLSAT 146
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
225-355 |
8.80e-09 |
|
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: 54.18 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 225 QKTGHRIQEELfYPSNEDKMALLQTLIEEEWP-DRAIIFANTKYKCESIwahlaADGHRVGLLTGDVPQKKREKILEQFT 303
Cdd:cd18789 18 GLGAHRKRRLL-AAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRY-----AKRLLKPFITGETPQSEREEILQNFR 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516400179 304 QGSVDLLVATDVAARGLhipqvthvfnyDLPD-DC-----------EDYVHRIGRTGRAGASGH 355
Cdd:cd18789 92 EGEYNTLVVSKVGDEGI-----------DLPEaNVaiqisghggsrRQEAQRLGRILRPKKGGG 144
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
33-167 |
5.41e-08 |
|
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: 52.65 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 33 TPIQALAL-PVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTtpaHEGRqptqprAIIMAPTRELAIQIYNDAEPLIAST 111
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALAT---SGGK------AVYIAPTRALVNQKEADLRERFGPL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 516400179 112 GIKAALAYGGESYDKQLAklqGGVDVLIGTTgRIIDF--YKQRVFNLNNIQAVVLDEA 167
Cdd:cd17921 74 GKNVGLLTGDPSVNKLLL---AEADILVATP-EKLDLllRNGGERLIQDVRLVVVDEA 127
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
293-351 |
1.36e-07 |
|
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: 48.47 E-value: 1.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 516400179 293 KKREKILEQFTqgsvdLLVATDVAARGLHIPQVTHVFNYDLPDDCEDYVHRIGRTGRAG 351
Cdd:cd18785 14 EHAEEIASSLE-----ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
258-349 |
1.48e-07 |
|
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: 50.43 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 258 RAIIFANTKYKCESIWAHLAAD----------GHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTH 327
Cdd:cd18801 32 RVIIFSEFRDSAEEIVNFLSKIrpgiratrfiGQASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDL 111
|
90 100
....*....|....*....|..
gi 516400179 328 VFNYDLPDDCEDYVHRIGRTGR 349
Cdd:cd18801 112 IICYDASPSPIRMIQRMGRTGR 133
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
243-352 |
3.58e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.57 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 243 KMALLQTLIEEEW---PD-RAIIFANTKYKCESIWAHLAADGHRVGLLTGD--------VPQKKREKILEQFTQGSVDLL 310
Cdd:PRK13766 348 KLEKLREIVKEQLgknPDsRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 516400179 311 VATDVAARGLHIPQVthvfnydlpddceDYV-------------HRIGRTGRAGA 352
Cdd:PRK13766 428 VSTSVAEEGLDIPSV-------------DLVifyepvpseirsiQRKGRTGRQEE 469
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
53-313 |
6.27e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 51.62 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 53 AQTGTGKTLAFLTATFNHLlttpahegRQPTQPRAIIMAPTRELAIQIYNDAEPLIastGIKAALAYG--GESYDKQLAK 130
Cdd:COG1203 154 APTGGGKTEAALLFALRLA--------AKHGGRRIIYALPFTSIINQTYDRLRDLF---GEDVLLHHSlaDLDLLEEEEE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 131 LQGGV------------DVLIGTTGRIIDF----YKQRVFNLNNIQ--AVVLDEADrMFDLGFIKDIRFLFRRMpapqER 192
Cdd:COG1203 223 YESEArwlkllkelwdaPVVVTTIDQLFESlfsnRKGQERRLHNLAnsVIILDEVQ-AYPPYMLALLLRLLEWL----KN 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 193 LN---MLFSATLSYRVQELAFEHM----HNPEHVVVEPEQKTGHRIQEELFYPSNEDKMALLQTLIEEEwpDRAIIFANT 265
Cdd:COG1203 298 LGgsvILMTATLPPLLREELLEAYelipDEPEELPEYFRAFVRKRVELKEGPLSDEELAELILEALHKG--KSVLVIVNT 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 516400179 266 KYKCESIWAHLAADGHRVG--LLTGDVPQKKREKILEQ----FTQGSVDLLVAT 313
Cdd:COG1203 376 VKDAQELYEALKEKLPDEEvyLLHSRFCPADRSEIEKEikerLERGKPCILVST 429
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
10-97 |
1.10e-06 |
|
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: 50.99 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 10 KFADL--GLNPQVVEGLEKKGFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPahegrqptQPRA 87
Cdd:COG1205 33 RYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP--------GATA 104
|
90
....*....|
gi 516400179 88 IIMAPTRELA 97
Cdd:COG1205 105 LYLYPTKALA 114
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
52-322 |
3.73e-06 |
|
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: 48.58 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 52 QAQTGTGKT-LAFLTAtfnhllttpAHEGRQPTQPRAIIMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESYDK---- 126
Cdd:cd09639 5 EAPTGYGKTeAALLWA---------LHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMgdse 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 127 ------------QLAKLQGGV-----DVLIGTTGRIIDFYKQRVFNLNNiQAVVLDEADRM--FDLGFIKDIRFLFRRMP 187
Cdd:cd09639 76 efehlfplyihsNDTLFLDPItvctiDQVLKSVFGEFGHYEFTLASIAN-SLLIFDEVHFYdeYTLALILAVLEVLKDND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 188 APQerlnMLFSATLSYRVQELaFEHMHNPE-HVVVEPEQKTGHRIQEELfypsNED--KMALLQTLIEE-EWPDRAIIFA 263
Cdd:cd09639 155 VPI----LLMSATLPKFLKEY-AEKIGYVEeNEPLDLKPNERAPFIKIE----SDKvgEISSLERLLEFiKKGGSVAIIV 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516400179 264 NTKYKCESIWAHLAADGHRVG--LLTGDVPQKKREK----ILEQFTQGSVDLLVATDVAARGLHI 322
Cdd:cd09639 226 NTVDRAQEFYQQLKEKGPEEEimLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
260-351 |
5.25e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 48.56 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 260 IIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHVFNYDLPDDCED 339
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90
....*....|..
gi 516400179 340 YVHRIGRTGRAG 351
Cdd:PRK11057 320 YYQETGRAGRDG 331
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
260-351 |
8.28e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 48.35 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 260 IIFANTKYKCESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHVFNYDLPDDCED 339
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|..
gi 516400179 340 YVHRIGRTGRAG 351
Cdd:PLN03137 764 YHQECGRAGRDG 775
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
36-186 |
2.62e-05 |
|
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: 44.50 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 36 QALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTPahegrqptQPRAIIMAPTRELAiqiyND-AEPLIA----- 109
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP--------GSRALYLYPTKALA----QDqLRSLRElleql 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 110 STGIKAALAYGGESYDKQLAKLQGGVDVLIgTTGRIIDF------YKQRVFnLNNIQAVVLDEAdRMFDLGFIKDIRFLF 183
Cdd:cd17923 73 GLGIRVATYDGDTPREERRAIIRNPPRILL-TNPDMLHYallphhDRWARF-LRNLRYVVLDEA-HTYRGVFGSHVALLL 149
|
...
gi 516400179 184 RRM 186
Cdd:cd17923 150 RRL 152
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
34-166 |
2.63e-05 |
|
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: 44.63 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 34 PIQALAL-PVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLttpahEGRqptqpRAIIMAPTRELAIQIYNDAEPLiASTG 112
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLL-----EGG-----KALYLVPLRALASEKYEEFKKL-EEIG 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 516400179 113 IKAALAYGgeSYDKQLAKLqGGVDVLIGTTGRIIDFYKQRVFNLNNIQAVVLDE 166
Cdd:cd18028 73 LKVGISTG--DYDEDDEWL-GDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
52-170 |
4.94e-05 |
|
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: 43.94 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 52 QAQTGTGKTLAFLTATFNHLlttpaHEGRQptqprAIIMAPTRELAIQIYNDAEPLIAStgIKAALAYGGESydkqlAKL 131
Cdd:cd17918 42 SGDVGSGKTLVALGAALLAY-----KNGKQ-----VAILVPTEILAHQHYEEARKFLPF--INVELVTGGTK-----AQI 104
|
90 100 110
....*....|....*....|....*....|....*....
gi 516400179 132 QGGVDVLIGTTGRIidfykQRVFNLNNIQAVVLDEADRM 170
Cdd:cd17918 105 LSGISLLVGTHALL-----HLDVKFKNLDLVIVDEQHRF 138
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
56-141 |
5.50e-05 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 45.53 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 56 GTGKTL-AFLTAtfnhLLTTPAheGRQptqprAIIMAPTRELAIQIYNDAEPLIASTGIKAALAYGGESY---DKQLAKL 131
Cdd:PRK10917 292 GSGKTVvAALAA----LAAIEA--GYQ-----AALMAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKGkerREILEAI 360
|
90
....*....|.
gi 516400179 132 Q-GGVDVLIGT 141
Cdd:PRK10917 361 AsGEADIVIGT 371
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
43-168 |
1.08e-04 |
|
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: 43.08 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 43 LLSGQDIAGQAQTGTGKTlAFLTATFNHLlttpAHEGRqptqpRAIIMAPTRELAIQIYNDAEPLIASTGIKA-ALAYGG 121
Cdd:cd17924 29 LLRGKSFAIIAPTGVGKT-TFGLATSLYL----ASKGK-----RSYLIFPTKSLVKQAYERLSKYAEKAGVEVkILVYHS 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 516400179 122 -------ESYDKQLAKlqGGVDVLIGTT---GRIIDFYKQRVFNLnniqaVVLDEAD 168
Cdd:cd17924 99 rlkkkekEELLEKIEK--GDFDILVTTNqflSKNFDLLSNKKFDF-----VFVDDVD 148
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
16-127 |
2.40e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 43.72 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 16 LNPQVVEGLEKKgFEFCTPIQALALPVLLSGQDIAGQAQTGTGKTLAFLTATFNHLLTTpAHEGRQPTQPRAIIMAPTRE 95
Cdd:PRK13767 18 LRPYVREWFKEK-FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRL-GREGELEDKVYCLYVSPLRA 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 516400179 96 LAIQIY-NDAEPLiasTGIKAALAYGGE---------------SYDKQ 127
Cdd:PRK13767 96 LNNDIHrNLEEPL---TEIREIAKERGEelpeirvairtgdtsSYEKQ 140
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
270-313 |
4.01e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 42.73 E-value: 4.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 516400179 270 ESIWAHLAADGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVAT 313
Cdd:COG1200 326 RSLSKLLEPLGIRVALLTGSTKAKERREILAALASGEADIVVGT 369
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
282-326 |
4.17e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 40.79 E-value: 4.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 516400179 282 RVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVT 326
Cdd:cd18811 63 NVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNAT 107
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
282-326 |
6.95e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.94 E-value: 6.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 516400179 282 RVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVT 326
Cdd:cd18792 62 RVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNAN 106
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
280-326 |
7.26e-04 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 42.03 E-value: 7.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 516400179 280 GHRVGLLTGDVPQKKR--EKILEQFTQGSVDLLVATDVAARGLHIPQVT 326
Cdd:COG1198 503 DARVLRMDRDTTRRKGalEKLLEAFARGEADILVGTQMLAKGHDFPNVT 551
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
282-313 |
1.08e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain] Cd Length: 225 Bit Score: 40.21 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|..
gi 516400179 282 RVGLLTGDVPQKKREKILEQFTQGSVDLLVAT 313
Cdd:cd17992 124 RVALLTGSTKAKEKREILEKIASGEIDIVIGT 155
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
292-367 |
1.11e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain] Cd Length: 238 Bit Score: 40.31 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 292 QKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHV--FNYD----LPDdcedyvHR------------IGRTGRAGAS 353
Cdd:cd18804 130 KGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADsglnSPD------FRaserafqlltqvSGRAGRGDKP 203
|
90
....*....|....*.
gi 516400179 354 GHSI--SFACEDYAIN 367
Cdd:cd18804 204 GKVIiqTYNPEHPLIQ 219
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
296-326 |
1.53e-03 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 40.91 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|.
gi 516400179 296 EKILEQFTQGSVDLLVATDVAARGLHIPQVT 326
Cdd:PRK05580 470 EQLLAQFARGEADILIGTQMLAKGHDFPNVT 500
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
35-166 |
2.18e-03 |
|
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: 39.26 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 35 IQALALPVLL-SGQDIAGQAQTGTGKTLAFLTAtFNHLLTTPahEGRQPTQPRAIIMAPTRELAIQIYNDAEPLIASTGI 113
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELA-ILRLLKER--NPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 516400179 114 KAALAYG-GESYDkqLAKLQgGVDVLIGTTGR---IIDFYKQRVFNLNNIQAVVLDE 166
Cdd:cd18023 82 SCAELTGdTEMDD--TFEIQ-DADIILTTPEKwdsMTRRWRDNGNLVQLVALVLIDE 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
260-349 |
2.52e-03 |
|
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: 38.40 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 260 IIFANTKYKCESIWAHLAA------DGHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDVAARGLHIPQVTHVFNYDL 333
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*.
gi 516400179 334 PDDCEDYVHRIGRTGR 349
Cdd:cd18796 122 PKSVARLLQRLGRSGH 137
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
217-357 |
4.03e-03 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 37.92 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 217 EHVVVEPEQKTgHRIQEELFYPSNEDKMALLQTLIEEEWPdrAIIFANTKYKCESIWAHLAADG-HRVGLLTGDvpqkkR 295
Cdd:cd18795 7 EYVLGFNGLGI-KLRVDVMNKFDSDIIVLLKIETVSEGKP--VLVFCSSRKECEKTAKDLAGIAfHHAGLTRED-----R 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516400179 296 EKILEQFTQGSVDLLVATDVAARGLHIPQVTHVFN----YDLPDDCE----DYVHRIGRTGRAG--ASGHSI 357
Cdd:cd18795 79 ELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYDGKGYRElsplEYLQMIGRAGRPGfdTRGEAI 150
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
282-313 |
4.40e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 39.36 E-value: 4.40e-03
10 20 30
....*....|....*....|....*....|..
gi 516400179 282 RVGLLTGDVPQKKREKILEQFTQGSVDLLVAT 313
Cdd:PRK10917 340 RVALLTGSLKGKERREILEAIASGEADIVIGT 371
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
52-169 |
5.28e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain] Cd Length: 225 Bit Score: 38.28 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 52 QAQTGTGKTL-AFLTAtfnhLLTTPAheGRQptqprAIIMAPTRELAIQIYNDAEPLIASTGIKAALAYG---GESYDKQ 127
Cdd:cd17992 72 QGDVGSGKTVvAALAM----LAAVEN--GYQ-----VALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGstkAKEKREI 140
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516400179 128 LAKLQGG-VDVLIGTTGRIidfYKQRVFnlNNIQAVVLDEADR 169
Cdd:cd17992 141 LEKIASGeIDIVIGTHALI---QEDVEF--HNLGLVIIDEQHR 178
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
270-315 |
5.67e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 38.88 E-value: 5.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 516400179 270 ESIWAHLAAD--GHRVGLLTGDVPQKKREKILEQFTQGSVDLLVATDV 315
Cdd:COG1200 491 EETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
55-167 |
8.38e-03 |
|
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: 37.25 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400179 55 TGTGKTL--AFLTATFNHLLTTPAHEGRqptqpRAIIMAPTRELAIQiynDAEPLIASTGIKAALAYGGESYDKQLAKLQ 132
Cdd:cd18034 25 TGSGKTLiaVMLIKEMGELNRKEKNPKK-----RAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKWTKERW 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 516400179 133 GGV----DVLIGTTGRIIDFYKQRVFNLNNIQAVVLDEA 167
Cdd:cd18034 97 KEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| |
