|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-416 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 586.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLfesDCSTTNAPSALVLA 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL---DPSRPRAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 81 PTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRML 160
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 161 DMGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERRKQELLSELIGK 240
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 241 KNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVINIDL 320
Cdd:COG0513 239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 321 PWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKIKRVYLEGYEVSNR---EVLIDKIGKKPAHLRRTR 397
Cdd:COG0513 319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEkrlERLKPKIKEKLKGKKAGR 398
|
410
....*....|....*....
gi 930453618 398 ANKPSGQATGEARAKNRSR 416
Cdd:COG0513 399 GGRPGPKGERKARRGKRRR 417
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-419 |
9.02e-144 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 417.67 E-value: 9.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLfesdcsTTNAPS----- 75
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHL------ITRQPHakgrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 76 ---ALVLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLV 152
Cdd:PRK10590 75 pvrALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 153 LDEADRMLDMGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERRKQE 232
Cdd:PRK10590 155 LDEADRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 233 LLSELIGKKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGL 312
Cdd:PRK10590 235 LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 313 PRVINIDLPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKIKRVYLEGYEVSnrevliDKIGKKP-A 391
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPD------PSIKAEPiQ 388
|
410 420
....*....|....*....|....*...
gi 930453618 392 HLRRTRANKPSGQATGEARAKNRSRISN 419
Cdd:PRK10590 389 NGRQQRGGGGRGQGGGRGQQQGQPRRGE 416
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
3-368 |
1.42e-129 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 381.84 E-value: 1.42e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKL----FesdcsttnAPSALV 78
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLdvkrF--------RVQALV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 79 LAPTRELAEQIANNFKDFAKYTQ-LKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEAD 157
Cdd:PRK11776 78 LCPTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 158 RMLDMGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTnSTASTVQHVVYPVEERRKQELLSEL 237
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVEST-HDLPAIEQRFYEVSPDERLPALQRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 238 IGKKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVIN 317
Cdd:PRK11776 237 LLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 930453618 318 IDLPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKIKR 368
Cdd:PRK11776 317 YELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNW 367
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-422 |
2.77e-118 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 351.94 E-value: 2.77e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAPSALVLA 80
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 81 PTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRML 160
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 161 DMGFINDMQSVIKSCADERQILLFSATFP-AAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERR-KQELLSELI 238
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 239 GKKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVINI 318
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 319 DLPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKIKRVYLEGYEVSNR---EVLIDKIGKKPAHLRR 395
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKapsEKKTGKPSKKVLAKRA 400
|
410 420
....*....|....*....|....*..
gi 930453618 396 TRANKPSGQATGEARAKNRSRISNVRK 422
Cdd:PRK11192 401 EKKEKEKEKPKVKKRHRDTKNIGKRRK 427
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-367 |
2.10e-111 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 335.73 E-value: 2.10e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTT---NAPSALVL 79
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 80 APTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEG-VDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADR 158
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 159 MLDMGFINDMQSVIKSC--ADERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERRKQELLSE 236
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTprKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 237 LIGKKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVI 316
Cdd:PRK01297 329 LVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 930453618 317 NIDLPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKIK 367
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-207 |
4.14e-104 |
|
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: 307.06 E-value: 4.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAPSALVLAPTRELAEQIAN 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 92 NFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQSV 171
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 930453618 172 IKSCADERQILLFSATFPAAIKQFASKVLKQPEIVR 207
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-416 |
6.98e-98 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 299.19 E-value: 6.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLF---ESDCSTTNAPSALVL 79
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLshpAPEDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 80 APTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRM 159
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 160 LDMGFINDMQSVIKSC--ADERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQH-VVYPVEERrKQELLSE 236
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEeLFYPSNEE-KMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 237 LIgKKNW-QQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRV 315
Cdd:PRK04837 249 LI-EEEWpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 316 INIDLPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKIKrvylegyeVS--NREVLIDKIgkkPAHL 393
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIP--------VSkyDSDALLTDL---PKPL 396
|
410 420
....*....|....*....|....
gi 930453618 394 RRTRANKPSG-QATGEARAKNRSR 416
Cdd:PRK04837 397 RLTRPRTGNGpRRSGAPRNRRRRK 420
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-382 |
3.53e-97 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 304.08 E-value: 3.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESdcstTNAPSALVLA 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE----LKAPQILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 81 PTRELAEQIANNFKDFAKYTQ-LKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRM 159
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 160 LDMGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERRKQELLSELIG 239
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 240 KKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVINID 319
Cdd:PRK11634 242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930453618 320 LPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKIKRVylegyEVSNREVL 382
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEV-----ELPNAELL 379
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
3-348 |
5.58e-93 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 290.52 E-value: 5.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALP-IIQKLFESDCSTTNAPSALVLAP 81
Cdd:PTZ00110 132 FEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPLLRYGDGPIVLVLAP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 82 TRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLD 161
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLD 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 162 MGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLK-QPEIVRVDQTNSTAS-TVQHVVYPVEERRKQELLSELIG 239
Cdd:PTZ00110 292 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKeEPVHVNVGSLDLTAChNIKQEVFVVEEHEKRGKLKMLLQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 240 K--KNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVIN 317
Cdd:PTZ00110 372 RimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVIN 451
|
330 340 350
....*....|....*....|....*....|.
gi 930453618 318 IDLPWLAEDYVHRIGRTGRAGNQGQAISFVS 348
Cdd:PTZ00110 452 FDFPNQIEDYVHRIGRTGRAGAKGASYTFLT 482
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-427 |
4.61e-87 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 276.06 E-value: 4.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAPS---AL 77
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKPEdprAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 78 VLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNL-SLAQVKHLVLDEA 156
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 157 DRMLDMGFINDMQSVIKSCADE--RQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERRKQELL 234
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 235 SELIGKKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPR 314
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 315 VINIDLPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEIETLIGQKI----------------KRVYLEGYEVSN 378
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIpvepvtaelltplprpPRVPVEGEEADD 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 930453618 379 REVliDKIGKKPAHLRRTRANKPSGQATGEARAKNRSRISNVRKSLKGE 427
Cdd:PRK04537 409 EAG--DSVGTIFREAREQRAAEEQRRGGGRSGPGGGSRSGSVGGGGRRD 455
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
3-201 |
3.87e-79 |
|
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: 243.93 E-value: 3.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNA------PSA 76
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRgrrkayPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 77 LVLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEA 156
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 930453618 157 DRMLDMGFINDMQSVIKSC----ADERQILLFSATFPAAIKQFASKVLK 201
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREIQRLAADFLK 210
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-358 |
1.05e-76 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 247.78 E-value: 1.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQK--LFESDCSTTN-APSAL 77
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGHPSEQrNPLAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 78 VLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEAD 157
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 158 RMLDMGFINDMQSVIKSCAdERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERRKQELLSEL 237
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 238 IGKKNWQQ--VLVFVNMKETADELVTELNL-DGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPR 314
Cdd:PLN00206 360 LKSKQHFKppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 930453618 315 VINIDLPWLAEDYVHRIGRTGRAGNQGQAISFVSREEENMLFEI 358
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-202 |
7.40e-70 |
|
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: 221.76 E-value: 7.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFE-----SDCSTTNAPS 75
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKegltaSSFSEVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 76 ALVLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDE 155
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 930453618 156 ADRMLDMGFINDMQSVIKSC----ADERQILLFSATFPAAIKQFASKVLKQ 202
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-207 |
7.99e-68 |
|
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: 214.48 E-value: 7.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 2 NFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESdcSTTNAPSALVLAP 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAH--SPTVGARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 82 TRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLD 161
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 930453618 162 MGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVR 207
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
27-372 |
8.93e-67 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 218.54 E-value: 8.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 27 IQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESdcstTNAPSALVLAPTRELAEQIANNFKDFAKYTQLKVVS 106
Cdd:PTZ00424 54 IQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD----LNACQALILAPTRELAQQIQKVVLALGDYLKVRCHA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 107 LFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQSVIKSCADERQILLFSA 186
Cdd:PTZ00424 130 CVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 187 TFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVE-ERRKQELLSELIGKKNWQQVLVFVNMKETADELVTELNL 265
Cdd:PTZ00424 210 TMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEkEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 266 DGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVINIDLPWLAEDYVHRIGRTGRAGNQGQAIS 345
Cdd:PTZ00424 290 RDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAIN 369
|
330 340
....*....|....*....|....*..
gi 930453618 346 FVSREEENMLFEIETLIGQKIKRVYLE 372
Cdd:PTZ00424 370 FVTPDDIEQLKEIERHYNTQIEEMPME 396
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-209 |
1.31e-66 |
|
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: 210.96 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDcSTTNAPSALVLAPTRELAEQIAN 91
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRP-KKKAATRVLVLVPTRELAMQCFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 92 NFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLG-NLSLAQVKHLVLDEADRMLDMGFINDMQS 170
Cdd:cd17947 80 VLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 930453618 171 VIKSCADERQILLFSATFPAAIKQFASKVLKQPeiVRVD 209
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP--VRVF 196
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
10-202 |
1.38e-63 |
|
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: 203.58 E-value: 1.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 10 PELIQALDELNYHTLTPIQRAAI-PAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAP-SALVLAPTRELAE 87
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGvSALIISPTRELAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 88 QIANNFKDFAKY-TQLKVVSLFGGVNTAGQEIAL-KEGVDVVVATPGRLLDHIR--LGNLSLAQVKHLVLDEADRMLDMG 163
Cdd:cd17964 83 QIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDMG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 930453618 164 FINDMQSVI----KSCADERQILLFSATFPAAIKQFASKVLKQ 202
Cdd:cd17964 163 FRPDLEQILrhlpEKNADPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
3-203 |
6.58e-63 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 201.78 E-value: 6.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESdcstTNAPSALVLAPT 82
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN----PQRFFALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 83 RELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHI-RLGNLSLAQVKHLVLDEADRMLD 161
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 930453618 162 MGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQP 203
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-195 |
1.02e-62 |
|
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: 199.78 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 25 TPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDcsttNAPSALVLAPTRELAEQIANNFKDFAKYTQLKV 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 105 VSLFGGVNTaGQEIALKEGVDVVVATPGRLLDHIRLGNLsLAQVKHLVLDEADRMLDMGFINDMQSVIKSCADERQILLF 184
Cdd:pfam00270 77 ASLLGGDSR-KEQLEKLKGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 930453618 185 SATFPAAIKQF 195
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-206 |
1.95e-60 |
|
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: 196.00 E-value: 1.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFE----SDCSTTNAPSALVLAPTRELAE 87
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 88 QIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFIND 167
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 930453618 168 MQSVI--------KSCADE------------RQILLFSATFPAAIKQFASKVLKQPEIV 206
Cdd:cd17945 161 VTKILdampvsnkKPDTEEaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-208 |
2.20e-60 |
|
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: 194.94 E-value: 2.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLF-ESDCSTTNAPSALVLAPTRELAEQIA 90
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMdQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 91 NNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQS 170
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 930453618 171 VIKSCADERQILLFSATFPAAIKQFASKVLKQPeiVRV 208
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDP--IRV 196
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-203 |
1.95e-59 |
|
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: 192.82 E-value: 1.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESdcsttnaPS---ALVL 79
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED-------PYgifALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 80 APTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNL---SLAQVKHLVLDEA 156
Cdd:cd17955 74 TPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 930453618 157 DRMLDMGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQP 203
Cdd:cd17955 154 DRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
12-205 |
5.11e-59 |
|
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: 192.21 E-value: 5.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTT-NAPSALVLAPTRELAEQIA 90
Cdd:cd17953 23 VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPgEGPIGLIMAPTRELALQIY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 91 NNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGN---LSLAQVKHLVLDEADRMLDMGFIND 167
Cdd:cd17953 103 VECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRMFDMGFEPQ 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 930453618 168 MQSVIKSCADERQILLFSATFPAAIKQFASKVLKQP-EI 205
Cdd:cd17953 183 IMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPiEI 221
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-208 |
2.03e-58 |
|
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: 190.11 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDcsTTNAPSALVLAPTRELAEQIAN 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR--KKKGLRALILAPTRELASQIYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 92 NFKDFAKYTQLKVVSLFGG-VNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQS 170
Cdd:cd17957 79 ELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 930453618 171 VIKSC-ADERQILLFSATFPAAIKQFASKVLKQPeiVRV 208
Cdd:cd17957 159 ILAACtNPNLQRSLFSATIPSEVEELARSVMKDP--IRI 195
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-205 |
1.12e-57 |
|
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: 188.28 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFesdcSTTNAPSALVLAPT 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID----PKKDVIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 83 RELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDM 162
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 930453618 163 GFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQP-EI 205
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPyEI 200
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-242 |
2.28e-57 |
|
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: 188.60 E-value: 2.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIP-AVRKGKDVLASAQTGTGKTAAFALPIIQKL-----FESDCSTTNAPSALVLAPTREL 85
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqksSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 86 AEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKH---LVLDEADRMLDM 162
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSlrfLVLDEADRMLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 163 GFINDMQSVIKSCADE-------RQILLFSATFpaaikqfaSKVLKQPEIVRVDQTNSTASTVQhvvypveerrKQELLS 235
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL--------TLDHQLPLKLNSKKKKKKKEKKQ----------KLELLI 222
|
....*..
gi 930453618 236 ELIGKKN 242
Cdd:cd17946 223 EKVGFRK 229
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
10-208 |
1.37e-56 |
|
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: 185.48 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 10 PELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFE--SDCSTTNAPSALVLAPTRELAE 87
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKakAESGEEQGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 88 QIANNFKDFAKYT--QLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSL-AQVKHLVLDEADRMLDMGF 164
Cdd:cd17961 83 QVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 930453618 165 INDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVRV 208
Cdd:cd17961 163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-206 |
1.50e-55 |
|
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: 182.91 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLfesdcsttnapSALVLAPT 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-----------VALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 83 RELAEQIANNFKDFAKYT---QLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRM 159
Cdd:cd17938 70 RELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 930453618 160 LDMG---FINDMQSVI-KSCADER--QILLFSATFPA-AIKQFASKVLKQPEIV 206
Cdd:cd17938 150 LSQGnleTINRIYNRIpKITSDGKrlQVIVCSATLHSfEVKKLADKIMHFPTWV 203
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-347 |
3.23e-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: 179.24 E-value: 3.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 219 QHVVYPVEERRKQELLSELIGKKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLV 298
Cdd:cd18787 3 QLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 930453618 299 ATEVAARGIDIDGLPRVINIDLPWLAEDYVHRIGRTGRAGNQGQAISFV 347
Cdd:cd18787 83 ATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-209 |
5.64e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 181.15 E-value: 5.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 16 LDELNYHTLTPIQRAAIPAVRKG-KDVLASAQTGTGKTAAFALPIIQKLFESdcsttNAPSALVLAPTRELAEQIANNFK 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-----KGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 95 DFAKYTQLKVVSLFGGVNTAGQEIALKEGV-DVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQSVIK 173
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 930453618 174 SCADERQILLFSATFPAAIKQFASKVLKQPEIVRVD 209
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG 191
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
11-200 |
6.79e-55 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 182.55 E-value: 6.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 11 ELIQALDEL-NYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNA------------PSAL 77
Cdd:cd18051 30 EIIRNNIELaRYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLPsesgyygrrkqyPLAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 78 VLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEAD 157
Cdd:cd18051 110 VLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEAD 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 930453618 158 RMLDMGFINDMQSVIKSCA----DERQILLFSATFPAAIKQFASKVL 200
Cdd:cd18051 190 RMLDMGFEPQIRRIVEQDTmpptGERQTLMFSATFPKEIQMLARDFL 236
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-203 |
2.54e-52 |
|
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: 174.09 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPII-----QKLFESDcsttNAPSALVLAPTRELA 86
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERG----DGPIVLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 87 EQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFIN 166
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 930453618 167 DMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQP 203
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
15-208 |
2.00e-51 |
|
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: 171.70 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 15 ALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAPSALVLAPTRELAEQIANNFK 94
Cdd:cd17941 4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 95 DFAKYTQLKVVSLFGGVNtAGQEIALKEGVDVVVATPGRLLDHI-RLGNLSLAQVKHLVLDEADRMLDMGFINDMQSVIK 173
Cdd:cd17941 84 KVGKYHSFSAGLIIGGKD-VKEEKERINRMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 930453618 174 SCADERQILLFSATFPAAIKQFASKVLKQPEIVRV 208
Cdd:cd17941 163 NLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
24-201 |
3.58e-49 |
|
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: 166.18 E-value: 3.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 24 LTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFES--DCSTTNAPSALVLAPTRELAEQIANNFKDFAKytQ 101
Cdd:cd17944 13 LFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDqqPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 102 LKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQSVI-----KSCA 176
Cdd:cd17944 91 LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSE 170
|
170 180
....*....|....*....|....*
gi 930453618 177 DERQILLFSATFPAAIKQFASKVLK 201
Cdd:cd17944 171 DNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
25-206 |
4.95e-49 |
|
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: 165.72 E-value: 4.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 25 TPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCS--TTNAPSALVLAPTRELAEQIANNFKDFaKYTQL 102
Cdd:cd17958 14 SPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPreQRNGPGVLVLTPTRELALQIEAECSKY-SYKGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 103 KVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQSVIKSCADERQIL 182
Cdd:cd17958 93 KSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDIRPDRQTI 172
|
170 180
....*....|....*....|....
gi 930453618 183 LFSATFPAAIKQFASKVLKQPEIV 206
Cdd:cd17958 173 MTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-208 |
5.27e-48 |
|
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: 163.28 E-value: 5.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDcsttNAPSALVLAPT 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD----GQVSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 83 RELAEQIANNFKDFAKY-TQLKVVSLFGGVNTAGQEIALK-EGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRM- 159
Cdd:cd17950 80 RELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMl 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 930453618 160 --LDMGfiNDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVRV 208
Cdd:cd17950 160 eqLDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
15-205 |
8.02e-48 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 162.53 E-value: 8.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 15 ALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAPSALVLAPTRELAEQIANNFK 94
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 95 DFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRL-GNLSLAQVKHLVLDEADRMLDMGFINDMQSVIK 173
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNtKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
|
170 180 190
....*....|....*....|....*....|..
gi 930453618 174 SCADERQILLFSATFPAAIKQFASKVLKQPEI 205
Cdd:cd17942 164 LLPKRRQTMLFSATQTRKVEDLARISLKKKPL 195
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
12-207 |
8.88e-48 |
|
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: 162.76 E-value: 8.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDE-LNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKL--FESDCSTTNAPSALVLAPTRELAEQ 88
Cdd:cd17949 1 LVSHLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlsLEPRVDRSDGTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 89 IANNFKDFAKYTQLKVV-SLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIR-LGNLSLAQVKHLVLDEADRMLDMGFIN 166
Cdd:cd17949 81 IYEVLEKLLKPFHWIVPgYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKnTQSFDVSNLRWLVLDEADRLLDMGFEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 930453618 167 DMQSVIK-------------SCADERQILLFSATFPAAIKQFASKVLKQPEIVR 207
Cdd:cd17949 161 DITKILEllddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
11-203 |
1.21e-47 |
|
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: 162.11 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 11 ELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLfesdCSTTNAPSALVLAPTRELAEQIA 90
Cdd:cd17939 7 DLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI----DTTVRETQALVLAPTRELAQQIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 91 NNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQS 170
Cdd:cd17939 83 KVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYD 162
|
170 180 190
....*....|....*....|....*....|...
gi 930453618 171 VIKSCADERQILLFSATFPAAIKQFASKVLKQP 203
Cdd:cd17939 163 IFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP 195
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-203 |
1.94e-47 |
|
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: 161.18 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQK-LFESDcsttnAPSALVLAPTRELAEQIA 90
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRcLTEHR-----NPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 91 NNFKDFAK-YTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQ 169
Cdd:cd17962 76 DQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....
gi 930453618 170 SVIKSCADERQILLFSATFPAAIKQFASKVLKQP 203
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-208 |
3.03e-47 |
|
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: 160.82 E-value: 3.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTT-NAPSALVLAPTRELAEQIA 90
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKkGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 91 NNFKDFAKYTQLKVVSLF--GGVNTAGQEIALKE-GVDVVVATPGRLLDHIRLGN--LSLAQVKHLVLDEADRMLDMGFI 165
Cdd:cd17960 81 EVLQSFLEHHLPKLKCQLliGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 930453618 166 NDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPeiVRV 208
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP--VRV 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-206 |
4.33e-46 |
|
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: 158.27 E-value: 4.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCST----TNAPSALVLAPTRELAE 87
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLpfikGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 88 QIANNFKDFAK------YTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLD 161
Cdd:cd17951 81 QTHEVIEYYCKalqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 930453618 162 MGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIV 206
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-202 |
1.32e-44 |
|
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: 155.17 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 1 MNFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPII-----QKLFESDcsttNAPS 75
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPFLERG----DGPI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 76 ALVLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDE 155
Cdd:cd18049 100 CLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 930453618 156 ADRMLDMGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQ 202
Cdd:cd18049 180 ADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
2-201 |
3.11e-43 |
|
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: 152.86 E-value: 3.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 2 NFKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKL-FESDCSTTNAPSALVLA 80
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHInHQPYLERGDGPICLVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 81 PTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRML 160
Cdd:cd18050 143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 930453618 161 DMGFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLK 201
Cdd:cd18050 223 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLR 263
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
10-207 |
1.09e-42 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 148.88 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 10 PELIQALDELNYHTLTPIQRAAIPAVRKG--KDVLASAQTGTGKTAAFALPIIQKLFESDcsttNAPSALVLAPTRELAE 87
Cdd:cd17963 3 PELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTL----KSPQALCLAPTRELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 88 QIANNFKDFAKYTQLKVVSLFggvntAGQEIALKEGVD--VVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDM-GF 164
Cdd:cd17963 79 QIGEVVEKMGKFTGVKVALAV-----PGNDVPRGKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 930453618 165 INDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVR 207
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-203 |
9.58e-41 |
|
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: 143.74 E-value: 9.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDcsttNAPSALVLAPT 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSL----KATQALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 83 RELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDM 162
Cdd:cd18046 77 RELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 930453618 163 GFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQP 203
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-187 |
1.47e-40 |
|
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: 144.31 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKG---------KDVLASAQTGTGKTAAFALPIIQKLfesdcSTTNAPS--ALVLA 80
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAL-----SKRVVPRlrALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 81 PTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEG--------VDVVVATPGRLLDHIRLG-NLSLAQVKHL 151
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTpGFTLKHLRFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 930453618 152 VLDEADRMLDMGFIN---------------DMQSVIKSCADER-----QILLFSAT 187
Cdd:cd17956 156 VIDEADRLLNQSFQDwletvmkalgrptapDLGSFGDANLLERsvrplQKLLFSAT 211
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-199 |
3.83e-39 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 140.58 E-value: 3.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTT---NAPSALVLAPTRELAEQ 88
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 89 IANNFKDFAKYTQLKVVSLFGGvNTAGQEIALK-EGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFIND 167
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGG-RTKRQIRNPHfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 930453618 168 MQSVIKSC---------ADER----QILLFSATFPAAIKQFASKV 199
Cdd:cd17948 160 LSHFLRRFplasrrsenTDGLdpgtQLVLVSATMPSGVGEVLSKV 204
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-207 |
3.18e-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: 134.31 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 12 LIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFesdcSTTNAPSALVLAPTRELAEQIAN 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD----LERRHPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 92 NFKDFAKY-TQLKVVSLFGGVNTAGQEIALKeGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFINDMQS 170
Cdd:cd17943 77 VFKKIGKKlEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 930453618 171 VIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVR 207
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-203 |
4.32e-36 |
|
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: 131.44 E-value: 4.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQkLFESdcsTTNAPSALVLAPT 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLDI---QVRETQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 83 RELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDM 162
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 930453618 163 GFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQP 203
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
230-338 |
3.93e-34 |
|
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: 123.09 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 230 KQELLSELIGKKNWQQVLVFVNMKETAD-ELVTELNldGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGID 308
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEaELLLEKE--GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 930453618 309 IDGLPRVINIDLPWLAEDYVHRIGRTGRAG 338
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
25-208 |
1.69e-31 |
|
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: 120.56 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 25 TPIQRAAIPAVRKG----------------KDVLASAQTGTGKTAAFALPIIQKLFESDCSTTN-------------APS 75
Cdd:cd17965 32 SPIQTLAIKKLLKTlmrkvtkqtsneepklEVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFEeaeeeyesakdtgRPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 76 ALVLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIAL--KEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVL 153
Cdd:cd17965 112 SVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLafKGRIDILVTTPGKLASLAKSRPKILSRVTHLVV 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 930453618 154 DEADRMLDMGFINDMQSVIKSCADERQILLFSATFPaaiKQFASKVLKQ-PEIVRV 208
Cdd:cd17965 192 DEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP---KEFDKTLRKLfPDVVRI 244
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
257-338 |
5.78e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 103.06 E-value: 5.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 257 DELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVINIDLPWLAEDYVHRIGRTGR 336
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 930453618 337 AG 338
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
23-315 |
2.24e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 102.41 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 23 TLTPIQRAAIPAV-----RKGKDVLASAQTGTGKTAAFALpIIQKLFESDcsttnapSALVLAPTRELAEQIANNFKDFa 97
Cdd:COG1061 80 ELRPYQQEALEALlaaleRGGGRGLVVAPTGTGKTVLALA-LAAELLRGK-------RVLVLVPRRELLEQWAEELRRF- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 98 kytqlkvvslFGGVNTAGQEIalKEGVDVVVATPGRLLDHIRLGNLSlAQVKHLVLDEADRMLDMGFindmQSVIKSCAD 177
Cdd:COG1061 151 ----------LGDPLAGGGKK--DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 178 ERqILLFSAT------FPAAIKQF-------------ASKVLKQPEIVRV-DQTNSTASTVQHVVYPVEER------RKQ 231
Cdd:COG1061 214 AY-RLGLTATpfrsdgREILLFLFdgivyeyslkeaiEDGYLAPPEYYGIrVDLTDERAEYDALSERLREAlaadaeRKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 232 ELLSELIGK-KNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDId 310
Cdd:COG1061 293 KILRELLREhPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV- 371
|
....*
gi 930453618 311 glPRV 315
Cdd:COG1061 372 --PRL 374
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-214 |
4.95e-23 |
|
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: 97.01 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 2 NFKSFSFAPELIQALDELNYHTLTPIQRAAIPAV--RKGKDVLASAQTGTGKTAAFALPIIQKLfesDCSTTnAPSALVL 79
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMlaDPPQNLIAQSQSGTGKTAAFVLAMLSRV---DALKL-YPQCLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 80 APTRELAEQIANNFKDFAKY-TQLKVVSLFGGvNTAGQEIALKEgvDVVVATPGRLLDH-IRLGNLSLAQVKHLVLDEAD 157
Cdd:cd18048 95 SPTFELALQTGKVVEEMGKFcVGIQVIYAIRG-NRPGKGTDIEA--QIVIGTPGTVLDWcFKLRLIDVTNISVFVLDEAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 930453618 158 RMLDM-GFINDMQSVIKSCADERQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNST 214
Cdd:cd18048 172 VMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
9-350 |
3.40e-22 |
|
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: 99.52 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 9 APELIQALDELNYHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTtnapsALVLAPTRELA-E 87
Cdd:COG1205 42 PPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT-----ALYLYPTKALArD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 88 QIAnNFKDFAKYTQLKV-VSLFGGvNTAGQE-IALKEGVDVVVATP-----GRLLDHIRLGNLsLAQVKHLVLDEA---- 156
Cdd:COG1205 117 QLR-RLRELAEALGLGVrVATYDG-DTPPEErRWIREHPDIVLTNPdmlhyGLLPHHTRWARF-FRNLRYVVIDEAhtyr 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 157 -----------DRMLDMgfindmqsviksCAD---ERQILLFSATfpaaI---KQFASKVLKQPeIVRVDQTNSTASTVQ 219
Cdd:COG1205 194 gvfgshvanvlRRLRRI------------CRHygsDPQFILASAT----IgnpAEHAERLTGRP-VTVVDEDGSPRGERT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 220 HV-----VYPVEERRKQ-----ELLSELIGKKnwQQVLVFVNMKETAdELVT-----ELNLDGIPAAVC--HGdksqG-- 280
Cdd:COG1205 257 FVlwnppLVDDGIRRSAlaeaaRLLADLVREG--LRTLVFTRSRRGA-ELLAryarrALREPDLADRVAayRA----Gyl 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 281 -NRRRAL-REFKEGKVRVLVAT---EVaarGIDIDGLPRVINIDLP------WlaedyvHRIGRTGRAGNQGQAIsFVSR 349
Cdd:COG1205 330 pEERREIeRGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPgtrasfW------QQAGRAGRRGQDSLVV-LVAG 399
|
.
gi 930453618 350 E 350
Cdd:COG1205 400 D 400
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-207 |
3.85e-20 |
|
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: 88.24 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 3 FKSFSFAPELIQALDELNYHTLTPIQRAAIPAV--RKGKDVLASAQTGTGKTAAFALPIIQKLfESDCSTTNApsaLVLA 80
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQV-EPANKYPQC---LCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 81 PTRELAEQIANNFKDFAKYtqLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDH-IRLGNLSLAQVKHLVLDEADRM 159
Cdd:cd18047 79 PTYELALQTGKVIEQMGKF--YPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 930453618 160 LDMGFINDMQSVI-----KSCaderQILLFSATFPAAIKQFASKVLKQPEIVR 207
Cdd:cd18047 157 IATQGHQDQSIRIqrmlpRNC----QMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
10-344 |
4.59e-20 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 92.27 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 10 PELIQALDELNYHTLTPIQRAAIPA-VRKGKDVLASAQTGTGKTAAFALPIIQKLFESdcsttnaPSALVLAPTRELAEQ 88
Cdd:COG1204 9 EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNG-------GKALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 89 IANNFKDFAKYTQLKVVSLFGGVNTAGQEIalkEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADrmldmgFINDM 168
Cdd:COG1204 82 KYREFKRDFEELGIKVGVSTGDYDSDDEWL---GRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAH------LIDDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 169 Q---------SVIKSCADERQILLFSATFPAAiKQFAS------------------KVLKQPEIVRVDQTNSTASTVQHV 221
Cdd:COG1204 153 SrgptlevllARLRRLNPEAQIVALSATIGNA-EEIAEwldaelvksdwrpvplneGVLYDGVLRFDDGSRRSKDPTLAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 222 VYP-VEERRkqellseligkknwqQVLVFVNMK----ETADELVTELNLDGIP--------------------------- 269
Cdd:COG1204 232 ALDlLEEGG---------------QVLVFVSSRrdaeSLAKKLADELKRRLTPeereeleelaeellevseethtnekla 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 270 ------AAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDidgLP--RVI--------NIDLPWLaeDYVHRIGR 333
Cdd:COG1204 297 dclekgVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVN---LParRVIirdtkrggMVPIPVL--EFKQMAGR 371
|
410
....*....|...
gi 930453618 334 TGRAG--NQGQAI 344
Cdd:COG1204 372 AGRPGydPYGEAI 384
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-187 |
3.32e-19 |
|
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: 83.61 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 38 GKDVLASAQTGTGKTAAFALPIIQKLfesdcsTTNAPSALVLAPTRELAEQIANNFKDFAKYTqlKVVSLFGGVNTAGQE 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL------LKKGKKVLVLVPTKALALQTAERLRELFGPG--IRVAVLVGGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930453618 118 IALKEG-VDVVVATPGRLLDHI-RLGNLSLAQVKHLVLDEADRMLDMGF--INDMQSVIKSCADERQILLFSAT 187
Cdd:cd00046 73 EKNKLGdADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRgaLILDLAVRKAGLKNAQVILLSAT 146
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
47-351 |
2.41e-17 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 84.40 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 47 TGTGKTAAFALPIIQKLFESDCSttnapsALVLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEiALKEGVDV 126
Cdd:COG1111 26 TGLGKTAVALLVIAERLHKKGGK------VLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRK-ELWEKARI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 127 VVATPGRLLDHIRLGNLSLAQVKHLVLDEADR--------------------MLDMGF---------------------- 164
Cdd:COG1111 99 IVATPQVIENDLIAGRIDLDDVSLLIFDEAHRavgnyayvyiaeryhedakdPLILGMtaspgsdeekieevcenlgien 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 165 ------------------------------INDMQSVIKSCADERQILLFSATFPAAIKQFASK------------VLKQ 202
Cdd:COG1111 179 vevrteedpdvapyvhdtevewirvelpeeLKEIRDLLNEVLDDRLKKLKELGVIVSTSPDLSKkdllalqkklqrRIRE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 203 P------------EIVRVD--------------------QTNSTAS--------------TVQHVVYPVEE--------R 228
Cdd:COG1111 259 DdsegyraisilaEALKLRhalelletqgveallrylerLEEEARSsggskaskrlvsdpRFRKAMRLAEEadiehpklS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 229 RKQELLSELIGKKNWQQVLVFVNMKETADELVTELNLDGIPA------AVCHGDK--SQGNRRRALREFKEGKVRVLVAT 300
Cdd:COG1111 339 KLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDKglTQKEQIEILERFRAGEFNVLVAT 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 930453618 301 EVAARGIDIDGLPRVINIDLPWLAEDYVHRIGRTGRaGNQGQAISFV---SREE 351
Cdd:COG1111 419 SVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIakgTRDE 471
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
23-191 |
4.78e-15 |
|
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: 73.06 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 23 TLTPIQRAAIPAVR-KGKDVLASAQTGTGKTAAFALPIIQKLFESDCSttnapsALVLAPTRELAEQIANNFKDFAKYTQ 101
Cdd:cd17921 1 LLNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSGGK------AVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 102 LKVVSLFGGVNTAGQEIALKegvDVVVATPGRLLDHIR-LGNLSLAQVKHLVLDEADrmldmgFIND------MQSVIKS 174
Cdd:cd17921 75 KNVGLLTGDPSVNKLLLAEA---DILVATPEKLDLLLRnGGERLIQDVRLVVVDEAH------LIGDgergvvLELLLSR 145
|
170 180
....*....|....*....|
gi 930453618 175 C---ADERQILLFSATFPAA 191
Cdd:cd17921 146 LlriNKNARFVGLSATLPNA 165
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
47-432 |
9.10e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 70.29 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 47 TGTGKTAAFALPIIQKLfesdcsTTNAPSALVLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEGvDV 126
Cdd:PRK13766 38 TGLGKTAIALLVIAERL------HKKGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAELWEKA-KV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 127 VVATPGRLLDHIRLGNLSLAQVKHLVLDEADR------------------------------------------------ 158
Cdd:PRK13766 111 IVATPQVIENDLIAGRISLEDVSLLIFDEAHRavgnyayvyiaeryhedaknplvlgltaspgsdeekikevcenlgieh 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 159 ----------------------------------------ML--------DMGFI------------NDMQSVIKSCADE 178
Cdd:PRK13766 191 vevrteddpdvkpyvhkvkiewvrvelpeelkeirdllneALkdrlkklkELGVIvsispdvskkelLGLQKKLQQEIAN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 179 RQILLFSA--TFPAAIK----------QFASKVLKQPEIVRVDQTNSTAS----------TVQHVVYPVEE--------R 228
Cdd:PRK13766 271 DDSEGYEAisILAEAMKlrhavelletQGVEALRRYLERLREEARSSGGSkaskrlvedpRFRKAVRKAKEldiehpklE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 229 RKQELLSELIGKKNWQQVLVFVNMKETADELVTELNLDGIPA------AVCHGDK--SQGNRRRALREFKEGKVRVLVAT 300
Cdd:PRK13766 351 KLREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVST 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 301 EVAARGIDIdglPRVinidlpwlaeDYV-------------HRIGRTGRaGNQGQAISFVS-------------REEENM 354
Cdd:PRK13766 431 SVAEEGLDI---PSV----------DLVifyepvpseirsiQRKGRTGR-QEEGRVVVLIAkgtrdeayywssrRKEKKM 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 355 LFEIETL------IGQKIKRVYLEGYEVSNREVLIDKIGKKPAHLRRTRANKPSGQATGEARAKNRSRI--------SNV 420
Cdd:PRK13766 497 KEELKNLkgilnkKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKIivdsrelrSNV 576
|
570
....*....|..
gi 930453618 421 RKSLKGEKLSLK 432
Cdd:PRK13766 577 ARHLKRLGAEVE 588
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
232-332 |
2.46e-11 |
|
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: 60.95 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 232 ELLSELIGKKnwQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGK--VRVLVATEVAARGIDI 309
Cdd:cd18793 18 ELLEELREPG--EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNL 95
|
90 100
....*....|....*....|....*....
gi 930453618 310 DGLPRVINIDLPWL------AEDYVHRIG 332
Cdd:cd18793 96 TAANRVILYDPWWNpaveeqAIDRAHRIG 124
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
222-346 |
2.69e-11 |
|
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: 61.07 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 222 VYPVEERRKQELLSELIGKKNWQQ-VLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVAT 300
Cdd:cd18794 8 VRPKDKKDEKLDLLKRIKVEHLGGsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 930453618 301 eVA-ARGIDIDGLPRVINIDLPWLAEDYVHRIGRTGRAGNQGQAISF 346
Cdd:cd18794 88 -VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
40-310 |
1.12e-10 |
|
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: 62.83 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 40 DVLASAQTGTGKT---AAFALPIIqKLFESDcsttnapSALVLAPTRELAEQIANNFKD-FAKYTQLKVVSLFGGVNTAG 115
Cdd:cd09639 1 LLVIEAPTGYGKTeaaLLWALHSL-KSQKAD-------RVIIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 116 QEIALKE-------GVDVVVATPGRL--LDHI-------------RLGNLSLAQvkhLVLDEADRMLD--MGFINDMQSV 171
Cdd:cd09639 73 DSEEFEHlfplyihSNDTLFLDPITVctIDQVlksvfgefghyefTLASIANSL---LIFDEVHFYDEytLALILAVLEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 172 IKscaDERQ-ILLFSATFPAAIKQFASKVL--------------KQPEIVRVDQTNStastvqhvvypvEERRKQELLSE 236
Cdd:cd09639 150 LK---DNDVpILLMSATLPKFLKEYAEKIGyveenepldlkpneRAPFIKIESDKVG------------EISSLERLLEF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 237 LIGKKnwqQVLVFVNMKETADELVTELNLDG--IPAAVCHGDKSQGNRRRA----LREFKEGKVRVLVATEVAARGIDID 310
Cdd:cd09639 215 IKKGG---SVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEASLDIS 291
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
39-156 |
5.48e-10 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 58.82 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 39 KDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAPSALVLAPTRELAEQIAnnfKDFAKYTQLKVVSLFGGVNTAGQEI 118
Cdd:cd18034 17 RNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQA---EAIRSHTDLKVGEYSGEMGVDKWTK 93
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 930453618 119 ALK----EGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEA 156
Cdd:cd18034 94 ERWkeelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
47-188 |
1.08e-09 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 56.55 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 47 TGTGKTAaFALPIIQKLFEsdcsttnaPSALVLAPTRELAEQIANNFKDFakyTQLKVVSLFGGVNTAGQEIAlkegvDV 126
Cdd:cd17926 27 TGSGKTL-TALALIAYLKE--------LRTLIVVPTDALLDQWKERFEDF---LGDSSIGLIGGGKKKDFDDA-----NV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930453618 127 VVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLDMGFindmqSVIKSCADERQILLFSATF 188
Cdd:cd17926 90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF-----SEILKELNAKYRLGLTATP 146
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
220-350 |
4.28e-09 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 58.23 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 220 HVVYPVEERRKQELLsELIGKKNWQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVA 299
Cdd:COG0514 208 EVVPKPPDDKLAQLL-DFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVA 286
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 930453618 300 TeVA-ARGIDIDGLPRVINIDLPWLAEDYVHRIGRTGRAGNQGQAISFVSRE 350
Cdd:COG0514 287 T-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-156 |
4.74e-09 |
|
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: 55.67 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 28 QRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLfESDCSTTnapsALVLAPTRELAEQIANNFKDFAKYTQLKV-VS 106
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSR----ALYLYPTKALAQDQLRSLRELLEQLGLGIrVA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930453618 107 LFGGVNTAGQEIAL-KEGVDVVVATPgRLLDHI----------RLGNLslaqvKHLVLDEA 156
Cdd:cd17923 80 TYDGDTPREERRAIiRNPPRILLTNP-DMLHYAllphhdrwarFLRNL-----RYVVLDEA 134
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
232-334 |
6.39e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 57.93 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 232 ELLSELIGKKnwQQVLVFVNMKETADELVTELNLDGIPAAVCHGDKSQGNRRRALREFKEGK--VRVLVATEVAARGIDI 309
Cdd:COG0553 540 ELLEELLAEG--EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNL 617
|
90 100 110
....*....|....*....|....*....|.
gi 930453618 310 DGLPRVINIDLPWL------AEDYVHRIGRT 334
Cdd:COG0553 618 TAADHVIHYDLWWNpaveeqAIDRAHRIGQT 648
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-158 |
6.76e-09 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 55.21 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 27 IQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLfesdcsTTNAPSALVLAPTRELAEQIANNFKDFAKyTQLKVVS 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRL------TKKGGKVLILAPSRPLVEQHAENLKRVLN-IPDKITS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 930453618 107 LFGGVNTAGQEIALKEGvDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADR 158
Cdd:cd18035 78 LTGEVKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-65 |
1.25e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 57.20 E-value: 1.25e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 930453618 21 YHTLTPIQRAAIPAVRKGKDVLASAQTGTGKT-AAFaLPIIQKLFE 65
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDELFR 74
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
243-347 |
3.15e-08 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 50.40 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 243 WQQVLVFVNMKETADELVTELNldgipaavchgdksqgnrrralrefkegkvrVLVATEVAARGIDIDGLPRVINIDLPW 322
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90 100
....*....|....*....|....*.
gi 930453618 323 LAEDYVHRIGRTGRAGN-QGQAISFV 347
Cdd:cd18785 52 SAASYIQRVGRAGRGGKdEGEVILFV 77
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
40-310 |
3.60e-08 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 55.15 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 40 DVLASAQTGTGKT---AAFALPIIqKLFESDcsttnapSALVLAPTRELAEQIANNFKDF--AKYTQLKVVSLFGGVNTA 114
Cdd:TIGR01587 1 LLVIEAPTGYGKTeaaLLWALHSI-KSQKAD-------RVIIALPTRATINAMYRRAKELfgSELVGLHHSSSFSRIKEM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 115 GQEIALKE-------GVDVVVATPGRL--LDHI-------------RLGNLSLAQvkhLVLDEADRMLD--MGFINDMQS 170
Cdd:TIGR01587 73 GDSEEFEHlfplyihSNDKLFLDPITVctIDQVlksvfgefghyefTLASIANSL---LIFDEVHFYDEytLALILAVLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 171 VIKscaDERQ-ILLFSATFPAAIKQFASKVL-----------------KQPEIVRVDQTNStastvqhvvypvEERRKQE 232
Cdd:TIGR01587 150 VLK---DNDVpILLMSATLPKFLKEYAEKIGyvefnepldlkeerrfeNHRFILIESDKVG------------EISSLER 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 233 LLSELIGKKnwqQVLVFVNMKETADELVTELNlDGIPAA---VCHGDKSQGNRRRA----LREFKEGKV-RVLVATEVAA 304
Cdd:TIGR01587 215 LLEFIKKGG---SIAIIVNTVDRAQEFYQQLK-EKAPEEeiiLYHSRFTEKDRAKKeaelLREMKKSNEkFVIVATQVIE 290
|
....*.
gi 930453618 305 RGIDID 310
Cdd:TIGR01587 291 ASLDIS 296
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
244-344 |
3.80e-08 |
|
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: 51.97 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 244 QQVLVFVNMKETADELVTEL--NLDGIPAA--VCHGDK------SQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLP 313
Cdd:cd18801 31 TRVIIFSEFRDSAEEIVNFLskIRPGIRATrfIGQASGksskgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
|
90 100 110
....*....|....*....|....*....|.
gi 930453618 314 RVINIDLPWLAEDYVHRIGRTGRaGNQGQAI 344
Cdd:cd18801 111 LIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
246-340 |
5.68e-08 |
|
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: 51.88 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 246 VLVFVNMKETADELVTEL------NLDGIPAAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVINID 319
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|.
gi 930453618 320 LPWLAEDYVHRIGRTGRAGNQ 340
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPGA 141
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
225-309 |
6.43e-08 |
|
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: 51.48 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 225 VEERRKQELLSELIGK-KNWQQVLVFVNMKETADELVTELNLDGIpaavcHGDKSQGNRRRALREFKEGKVRVLVATEVA 303
Cdd:cd18789 30 AMNPNKLRALEELLKRhEQGDKIIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVSKVG 104
|
....*.
gi 930453618 304 ARGIDI 309
Cdd:cd18789 105 DEGIDL 110
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
11-159 |
6.69e-08 |
|
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: 52.03 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 11 ELIQALDELNYHTLTPIQRAAIPAVRKG------KDVLASAQTGTGKTAAFALPIIQKLfesdcstTNAPSALVLAPTRE 84
Cdd:cd17918 3 ALIQELCKSLPFSLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAY-------KNGKQVAILVPTEI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930453618 85 LAEQIANNFKDFakYTQLKVVSLfggvnTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAqvkhlVLDEADRM 159
Cdd:cd17918 76 LAHQHYEEARKF--LPFINVELV-----TGGTKAQILSGISLLVGTHALLHLDVKFKNLDLV-----IVDEQHRF 138
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
22-189 |
7.09e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.90 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 22 HTLTPIQRAAIPAVRKG-----KDVLASAQTGTGKT--AAFalpIIQKLFESdcstTNAPSALVLAPTRELAEQIANNFK 94
Cdd:pfam04851 2 LELRPYQIEAIENLLESikngqKRGLIVMATGSGKTltAAK---LIARLFKK----GPIKKVLFLVPRKDLLEQALEEFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 95 DFakytqLKVVSLFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVL--DEADRmldmGFINDMQSVI 172
Cdd:pfam04851 75 KF-----LPNYVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGASSYRNIL 145
|
170
....*....|....*..
gi 930453618 173 KSCaDERQILLFSATFP 189
Cdd:pfam04851 146 EYF-KPAFLLGLTATPE 161
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
27-316 |
9.63e-08 |
|
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: 53.93 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 27 IQRAAIPAVRKGK-DVLASAQTGTGKT---AAFALPIIQKlfesdcstTNAPSALVLAPTRELAEQianNFKDFAKYTQL 102
Cdd:COG1203 135 ALELALEAAEEEPgLFILTAPTGGGKTeaaLLFALRLAAK--------HGGRRIIYALPFTSIINQ---TYDRLRDLFGE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 103 KVV---SLFGGVNTAGQEIA---------LKEGVD--VVVAT------------PGRLLDHIRLGNlslaqvKHLVLDEA 156
Cdd:COG1203 204 DVLlhhSLADLDLLEEEEEYesearwlklLKELWDapVVVTTidqlfeslfsnrKGQERRLHNLAN------SVIILDEV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 157 D----RMLDMgfINDMQSVIKSCAdeRQILLFSATFPAAIKQFASKVLKQPEIVRVDQTNSTASTVQHVVYPVEERRKQE 232
Cdd:COG1203 278 QayppYMLAL--LLRLLEWLKNLG--GSVILMTATLPPLLREELLEAYELIPDEPEELPEYFRAFVRKRVELKEGPLSDE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 233 LLSELIGKK--NWQQVLVFVNMKETADELVTELNLDGIPAAVC--HGDKSQGNRRRALRE----FKEGKVRVLVATEVAA 304
Cdd:COG1203 354 ELAELILEAlhKGKSVLVIVNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRSEIEKEikerLERGKPCILVSTQVVE 433
|
330
....*....|..
gi 930453618 305 RGIDIDgLPRVI 316
Cdd:COG1203 434 AGVDID-FDVVI 444
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-189 |
1.03e-07 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 51.97 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 27 IQRAAIPAVRKG-KDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAPSALVLAPTRELAEQIANNFKdfAKYTQ--LK 103
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWK--EKFGPlgLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 104 VVSLFG-GVNTAGQEIalkEGVDVVVATP-------------GRLLDHIRLgnLSLAQVkHLVLDE--------ADRMLD 161
Cdd:cd18023 83 CAELTGdTEMDDTFEI---QDADIILTTPekwdsmtrrwrdnGNLVQLVAL--VLIDEV-HIIKENrgatlevvVSRMKT 156
|
170 180
....*....|....*....|....*...
gi 930453618 162 MGFinDMQSVIKSCADERQILLfSATFP 189
Cdd:cd18023 157 LSS--SSELRGSTVRPMRFVAV-SATIP 181
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
15-308 |
6.00e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 51.82 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 15 ALDELNYH------------TLTPIQRAAIPA-VRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTtnapsaLVLAP 81
Cdd:COG1202 189 PVDDLDLPpelkdllegrgeELLPVQSLAVENgLLEGKDQLVVSATATGKTLIGELAGIKNALEGKGKM------LFLVP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 82 TRELAEQIANNFKDfaKYTQLKVVSLFGGVNtagqEIALKEG-----VDVVVAT-PGrlLDH-IRLGNlSLAQVKHLVLD 154
Cdd:COG1202 263 LVALANQKYEDFKD--RYGDGLDVSIRVGAS----RIRDDGTrfdpnADIIVGTyEG--IDHaLRTGR-DLGDIGTVVID 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 155 EAdRMLDMG----FINDMQSVIKSCADERQILLFSAT--FPAAI-KQFASKVLKQPE----IVRvdqtnstastvqHVVY 223
Cdd:COG1202 334 EV-HMLEDPerghRLDGLIARLKYYCPGAQWIYLSATvgNPEELaKKLGAKLVEYEErpvpLER------------HLTF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 224 pVEERRKQELLSELIgKKNWQ---------QVLVFVNMKETADELVTELnldGIPAAVCHGDKSQGNRRRALREFKEGKV 294
Cdd:COG1202 401 -ADGREKIRIINKLV-KREFDtksskgyrgQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQEL 475
|
330
....*....|....
gi 930453618 295 RVLVATEVAARGID 308
Cdd:COG1202 476 AAVVTTAALAAGVD 489
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
23-191 |
6.15e-07 |
|
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: 49.25 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 23 TLTPIQRAAIPA-VRKGKDVLASAQTGTGKTAAFALPIIQKLFESDcsttnapSALVLAPTRELAEQIANNFKDFAKYtQ 101
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG-------KALYLVPLRALASEKYEEFKKLEEI-G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 102 LKVVSLFGGVNTAGQEIALKegvDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEadrmldMGFINDMQ---------SVI 172
Cdd:cd18028 73 LKVGISTGDYDEDDEWLGDY---DIIVATYEKFDSLLRHSPSWLRDVGVVVVDE------IHLISDEErgptlesivARL 143
|
170
....*....|....*....
gi 930453618 173 KSCADERQILLFSATFPAA 191
Cdd:cd18028 144 RRLNPNTQIIGLSATIGNP 162
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
26-158 |
1.07e-06 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 48.33 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 26 PIQRAAIPAV----RKGKD-VLASAQTGTGKT--AAFalpIIQKLFESdcstTNAPSALVLAPTRELAEQIANNFKdfak 98
Cdd:cd18032 3 YYQQEAIEALeearEKGQRrALLVMATGTGKTytAAF---LIKRLLEA----NRKKRILFLAHREELLEQAERSFK---- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 99 ytQLKVVSLFGGVNTAGQEIalkEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADR 158
Cdd:cd18032 72 --EVLPDGSFGNLKGGKKKP---DDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
16-352 |
1.32e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 50.59 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 16 LDELNYHTLTPIQRAAIPA-VRKGKDVLASAQTGTGKTAAFALPIIQKLFESdcsttnAPSALVLAPTRELAEQIANNFK 94
Cdd:PRK00254 16 LKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLRE------GGKAVYLVPLKALAEEKYREFK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 95 DFAKYTqLKVVSLFGGVNTAGQEIAlkeGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEA------DRMLDMGFIndm 168
Cdd:PRK00254 90 DWEKLG-LRVAMTTGDYDSTDEWLG---KYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIhligsyDRGATLEMI--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 169 qsvIKSCADERQILLFSATFPAAiKQFASKVlkQPEIVRVDQTnstastvqhvvyPVEERRKQELLSELI---GK----- 240
Cdd:PRK00254 163 ---LTHMLGRAQILGLSATVGNA-EELAEWL--NAELVVSDWR------------PVKLRKGVFYQGFLFwedGKierfp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 241 KNW-----------QQVLVFVNMKETADELVTEL---------------------NLDGIPA------------AVCHGD 276
Cdd:PRK00254 225 NSWeslvydavkkgKGALVFVNTRRSAEKEALELakkikrfltkpelralkeladSLEENPTneklkkalrggvAFHHAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 277 KSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLpRVINIDLPWLAEDYVHRI---------GRTGRA--GNQGQAIs 345
Cdd:PRK00254 305 LGRTERVLIEDAFREGLIKVITATPTLSAGINLPAF-RVIIRDTKRYSNFGWEDIpvleiqqmmGRAGRPkyDEVGEAI- 382
|
....*..
gi 930453618 346 FVSREEE 352
Cdd:PRK00254 383 IVATTEE 389
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
30-158 |
2.29e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 45.12 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 30 AAIPAVrKGKDVLASAQTGTGKTAAfALPIIQKLFESDCStTNAPSALVLAPTRELAEQIANNFKDFAKYTQLKVVSLFG 109
Cdd:cd17927 10 LAQPAL-KGKNTIICLPTGSGKTFV-AVLICEHHLKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 930453618 110 GVNT---AGQEIalkEGVDVVVATPGRLLDHIRLGNL-SLAQVKHLVLDEADR 158
Cdd:cd17927 87 DTSEnvsVEQIV---ESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDECHN 136
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
232-339 |
1.12e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 42.24 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 232 ELLSELIGKKnwQQVLVFVN--------MKETADELVTELNLDGIPAAVcHGDKSQGNRRRALREFKEGKVRVLVATEVA 303
Cdd:cd18797 26 RLFADLVRAG--VKTIVFCRsrklaellLRYLKARLVEEGPLASKVASY-RAGYLAEDRREIEAELFNGELLGVVATNAL 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 930453618 304 ARGIDIDGLPRVINIDLPWLAEDYVHRIGRTGRAGN 339
Cdd:cd18797 103 ELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGK 138
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
24-205 |
1.15e-04 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 42.64 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 24 LTPIQRAAIPAVRKGKDVLASAQTGTGKT--AAFALPIIQKlfesdcsttNAPSALVLAPTRELAEQianNFKDFaKYTq 101
Cdd:cd18027 9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQK---------HMTRTIYTSPIKALSNQ---KFRDF-KNT- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 102 lkvvslFGGVNTAGQEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADrmldmgFINDM------QSVIKSC 175
Cdd:cd18027 75 ------FGDVGLITGDVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVH------YINDAergvvwEEVLIML 142
|
170 180 190
....*....|....*....|....*....|..
gi 930453618 176 ADERQILLFSATFPAAIkQFASKV--LKQPEI 205
Cdd:cd18027 143 PDHVSIILLSATVPNTV-EFADWIgrIKKKNI 173
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
23-223 |
1.76e-04 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 42.43 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 23 TLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTNAP-SALVLAPTRELAEQiannFKDfakytq 101
Cdd:cd18024 32 TLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQRVIYTSPiKALSNQKYRELQEE----FGD------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 102 lkvVSLFGGvntagqEIALKEGVDVVVATPGRLLDHIRLGNLSLAQVKHLVLDEADRMLD--MGFINDmQSVIKSCADER 179
Cdd:cd18024 102 ---VGLMTG------DVTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRDkeRGVVWE-ETIILLPDKVR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 930453618 180 QILLfSATFPAAiKQFA---SKVLKQPeivrvdqtnstastvQHVVY 223
Cdd:cd18024 172 YVFL-SATIPNA-RQFAewiCKIHKQP---------------CHVVY 201
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
22-158 |
2.38e-04 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350749 [Multi-domain] Cd Length: 193 Bit Score: 41.79 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 22 HTLTPIQRAAIPAVRK----GK--DVLASAQTGTGKT-----AAFalpiiqklfesdCSTTNAPSALVLAPTRELAEQIA 90
Cdd:cd17991 14 YEETPDQLKAIEEILKdmesGKpmDRLICGDVGFGKTevamrAAF------------KAVLSGKQVAVLVPTTLLAQQHY 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930453618 91 NNFKDFAKYTQLKVVSLFGGVNTAGQEIALKEG----VDVVVATPGRLLDHIRLGNLSLaqvkhLVLDEADR 158
Cdd:cd17991 82 ETFKERFANFPVNVELLSRFTTAAEQREILEGLkegkVDIVIGTHRLLSKDVEFKNLGL-----LIIDEEQR 148
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
38-195 |
2.98e-04 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 41.51 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 38 GKDVLASAQTGTGKTAAfALPIIQKLFEsdcstTNAPSALVLA-PTRELAEQIANNFKDFAKY--TQLKVVSLFGGVNTA 114
Cdd:cd17930 1 PGLVILEAPTGSGKTEA-ALLWALKLAA-----RGGKRRIIYAlPTRATINQMYERIREILGRldDEDKVLLLHSKAALE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 115 GQEIALKEGVD------------------VVVATPGRLLD--------HIRLGNLSLAQVkhlVLDEA----DRMLDM-- 162
Cdd:cd17930 75 LLESDEEPDDDpveavdwalllkrswlapIVVTTIDQLLEsllkykhfERRLHGLANSVV---VLDEVqaydPEYMALll 151
|
170 180 190
....*....|....*....|....*....|...
gi 930453618 163 GFINDMQSVIKScaderQILLFSATFPAAIKQF 195
Cdd:cd17930 152 KALLELLGELGG-----PVVLMTATLPALLRDE 179
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
222-389 |
3.82e-04 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 41.14 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 222 VYPVEERRKQELLSELigKKNWQQVLVFVNM---KETADELVTELNLDGIPAAVCHGDksqgnRRRALREFKEGKVRVLV 298
Cdd:cd18798 5 VYIEDSDSLEKLLELV--KKLGDGGLIFVSIdygKEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 299 ATE----VAARGIDidgLPRVIN----IDLPwlAEDYVHRIGRTGR--AGNQGQAISFVSREEENmLFEIetlIGQKIKR 368
Cdd:cd18798 78 GVAsyygVLVRGID---LPERIKyaifYGVP--VTTYIQASGRTSRlyAGGLTKGLSVVLVDDPE-LFEA---LKKRLKL 148
|
170 180
....*....|....*....|.
gi 930453618 369 VYLEGYEVSNREVLIDKIGKK 389
Cdd:cd18798 149 ILDEFIFKELEEVDLEELLSE 169
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-155 |
4.80e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 40.64 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 38 GKDVLASAQTGTGKTAAFALPIIQKLFESDCSTTnapSALVLAPTRELAEQIANNFKDFAK--YTQLKVVSLFGGVNTAG 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV---QVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 930453618 116 QEIALKEGVDVVVATP---GRLLDHIRLGNLsLAQVKHLVLDE 155
Cdd:cd17922 78 KAKQLKNPPGILITTPeslELLLVNKKLREL-FAGLRYVVVDE 119
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
232-339 |
5.67e-04 |
|
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: 39.88 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 232 ELLSELIGKKNWQQVLVFVNMKETA---DELVTE--LNLDGIPAAVCHGDKSQGNRRRA----------LREFKEGKVRV 296
Cdd:cd18802 14 EILREYFPKTPDFRGIIFVERRATAvvlSRLLKEhpSTLAFIRCGFLIGRGNSSQRKRSlmtqrkqketLDKFRDGELNL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 930453618 297 LVATEVAARGIDIDGLPRVINIDLPWLAEDYVHRIGRtGRAGN 339
Cdd:cd18802 94 LIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
244-344 |
7.87e-04 |
|
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: 39.84 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 244 QQVLVFVNMKETADELVTELNldGIpaAVCHGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDidgLP--RVI----- 316
Cdd:cd18795 44 KPVLVFCSSRKECEKTAKDLA--GI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVN---LParTVIikgtq 116
|
90 100 110
....*....|....*....|....*....|....
gi 930453618 317 ---NIDLPWL-AEDYVHRIGRTGRAG--NQGQAI 344
Cdd:cd18795 117 rydGKGYRELsPLEYLQMIGRAGRPGfdTRGEAI 150
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
221-354 |
1.33e-03 |
|
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: 39.17 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 221 VVYP-VEERRKQELLSeligkknwqqvlvFVNMKETADELVTELNLdgipaAVCHGDKSQGNRRRALREFKEGKVRVLVA 299
Cdd:cd18792 31 YVYPrIEESEKLDLKS-------------IEALAEELKELVPEARV-----ALLHGKMTEDEKEAVMLEFREGEYDILVS 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 300 TEVAARGIDIdglPR-----VINIDLPWLAEDYVHRiGRTGRAGNQGQAIsFVSREEENM 354
Cdd:cd18792 93 TTVIEVGIDV---PNantmiIEDADRFGLSQLHQLR-GRVGRGKHQSYCY-LLYPDPKKL 147
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
220-340 |
1.74e-03 |
|
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: 38.86 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 220 HVVYP-VEErrkqellSELIGKKNWQQVlvfvnMKETADELVTELNLdgipaAVCHGDKSQGNRRRALREFKEGKVRVLV 298
Cdd:cd18811 30 YVIYPlIEE-------SEKLDLKAAVAM-----YEYLKERFRPELNV-----GLLHGRLKSDEKDAVMAEFREGEVDILV 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 930453618 299 ATEVAARGIDIdglPR-----VINIDLPWLAEdyVHRI-GRTGRAGNQ 340
Cdd:cd18811 93 STTVIEVGVDV---PNatvmvIEDAERFGLSQ--LHQLrGRVGRGDHQ 135
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
21-58 |
1.82e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 39.44 E-value: 1.82e-03
10 20 30
....*....|....*....|....*....|....*...
gi 930453618 21 YHTLTPIQRAAIPAVRKGKDVLASAQTGTGKTAAFALP 58
Cdd:cd17920 10 YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP 47
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
26-131 |
1.83e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 39.16 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 26 PIQRAAIPAVRKGKD-VLASAQTGTGKTAAFALPIIQklfesdCSTTNAPSALV-LAPTRELAEQIANNFKD-FAKYTQL 102
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLR------HWRQNPKGRAVyIAPMQELVDARYKDWRAkFGPLLGK 79
|
90 100
....*....|....*....|....*....
gi 930453618 103 KVVSLFGgvnTAGQEIALKEGVDVVVATP 131
Cdd:cd18021 80 KVVKLTG---ETSTDLKLLAKSDVILATP 105
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
20-155 |
3.13e-03 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 38.89 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 20 NYHTLTPIQRAAIP-AVRKGKDVLASAQTGTGKTAAFALPI---IQKLFESDCS-TTNAPSALVLAPTRELAEQIANNFK 94
Cdd:cd18019 14 GFKSLNRIQSKLFPaAFETDENLLLCAPTGAGKTNVALLTIlreIGKHRNPDGTiNLDAFKIVYIAPMKALVQEMVGNFS 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930453618 95 DFAKYTQLKVVSLFGGVNTAGQEIalkEGVDVVVATPGRlLDHI--RLGNLSLAQ-VKHLVLDE 155
Cdd:cd18019 94 KRLAPYGITVAELTGDQQLTKEQI---SETQIIVTTPEK-WDIItrKSGDRTYTQlVRLIIIDE 153
|
|
| HsdR |
COG4096 |
Type I site-specific restriction endonuclease, part of a restriction-modification system ... |
28-96 |
4.06e-03 |
|
Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];
Pssm-ID: 443272 [Multi-domain] Cd Length: 806 Bit Score: 39.44 E-value: 4.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930453618 28 QRAAIPAV----RKGKD----VLAsaqTGTGKTA-AFAlpIIQKLFESDcsttNAPSALVLAPTRELAEQIANNFKDF 96
Cdd:COG4096 163 QIEAIRRVeeaiAKGQRrallVMA---TGTGKTRtAIA--LIYRLLKAG----RAKRILFLADRNALVDQAKNAFKPF 231
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
48-155 |
7.95e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 38.59 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930453618 48 GTGKT--AAFA-LPIIQKLFESdcsttnapsALvLAPTRELAEQIANNFKDFAKYTQLKVVSLFGGVNTAGQEIALKE-- 122
Cdd:PRK10917 292 GSGKTvvAALAaLAAIEAGYQA---------AL-MAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKGKERREILEAia 361
|
90 100 110
....*....|....*....|....*....|....*
gi 930453618 123 --GVDVVVATPGRLLDHIRLGNLSLAqvkhlVLDE 155
Cdd:PRK10917 362 sgEADIVIGTHALIQDDVEFHNLGLV-----IIDE 391
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
274-335 |
8.00e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 38.75 E-value: 8.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930453618 274 HGDKSQGNRRRALREFKEGKVRVLVATEVAARGIDIDGLPRVINIDLPWLAEDYVHRIGRTG 335
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| |
